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Literature summary for 3.6.4.B6 extracted from

  • Meshcheryakov, V.A.; Wolf, M.
    Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly (2016), Protein Sci., 25, 1147-1155 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B6

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme FlaH, X-ray diffraction structure determination and analysis at 2.2 A resolution. FlaH crystals have been obtained in the absence of ATP or its analogues. Co-crystallization or postsoaking attempts were unsuccessful Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
ATP ATP affects the interaction between FlaH and the archaeal motor protein FlaI. In the presence of ATP, the FlaH-FlaI interaction becomes significantly weaker Methanocaldococcus jannaschii

Localization

Localization Comment Organism GeneOntology No. Textmining
flagellum
-
 Methanocaldococcus jannaschii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Methanocaldococcus jannaschii enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker ?
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additional information Methanocaldococcus jannaschii NBRC 100440 enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker ?
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additional information Methanocaldococcus jannaschii DSM 2661 enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker ?
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additional information Methanocaldococcus jannaschii ATCC 43067 enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker ?
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additional information Methanocaldococcus jannaschii JAL-1 enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker ?
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additional information Methanocaldococcus jannaschii JCM 10045 enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker ?
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Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58309 i.e. Methanococcus jannaschii
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Methanocaldococcus jannaschii ATCC 43067 Q58309 i.e. Methanococcus jannaschii
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Methanocaldococcus jannaschii DSM 2661 Q58309 i.e. Methanococcus jannaschii
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Methanocaldococcus jannaschii JAL-1 Q58309 i.e. Methanococcus jannaschii
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Methanocaldococcus jannaschii JCM 10045 Q58309 i.e. Methanococcus jannaschii
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Methanocaldococcus jannaschii NBRC 100440 Q58309 i.e. Methanococcus jannaschii
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker Methanocaldococcus jannaschii ?
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additional information FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii ?
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additional information enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker Methanocaldococcus jannaschii NBRC 100440 ?
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-
additional information FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii NBRC 100440 ?
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-
additional information enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker Methanocaldococcus jannaschii DSM 2661 ?
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-
additional information FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii DSM 2661 ?
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-
additional information enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker Methanocaldococcus jannaschii ATCC 43067 ?
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additional information FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii ATCC 43067 ?
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additional information enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker Methanocaldococcus jannaschii JAL-1 ?
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-
additional information FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii JAL-1 ?
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-
additional information enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker Methanocaldococcus jannaschii JCM 10045 ?
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-
additional information FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii JCM 10045 ?
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Subunits

Subunits Comment Organism
More enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
flagellar accessory protein
-
 Methanocaldococcus jannaschii
FlaH
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Methanocaldococcus jannaschii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 assay at Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
additional information FlaH binds to immobilized ATP and can be specifically eluted by addition of free ATP. The ATP-binding site is the most conserved region on the FlaH surface, suggesting that ATP binding is an essential property of FlaH proteins. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function Methanocaldococcus jannaschii

General Information

General Information Comment Organism
evolution the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria Methanocaldococcus jannaschii
additional information a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins Methanocaldococcus jannaschii
physiological function the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system Methanocaldococcus jannaschii