Literature summary for 6.3.5.13 extracted from

Noeldeke, E.R.; Muckenfuss, L.M.; Niemann, V.; Mueller, A.; Stoerk, E.; Zocher, G.; Schneider, T.; Stehle, T.
Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus (2018), Sci. Rep., 8, 12953 .

Search for more literature for 6.3.5.13

Cloned(Commentary)

Cloned (Comment)	Organism
-	Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the GatD/MurT complex reveals an open, boomerang-shaped conformation in which GatD is docked onto one end of MurT. Putative active site residues cluster at the interface between GatD and MurT and are contributed by both proteins	Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
C94S	subunit GatD mutant, complete loss of activity	Staphylococcus aureus
D349N	subunit Murt mutant, displays severely reduced in vitro activity	Staphylococcus aureus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
72000	-	gel filtration	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	A0A0H3JN63 and A0A0H3JUU7	A0A0H3JN63 i.e subunit GatD, A0A0H3JUU7 i.e. subunit MurT	-
Staphylococcus aureus N315	A0A0H3JN63 and A0A0H3JUU7	A0A0H3JN63 i.e subunit GatD, A0A0H3JUU7 i.e. subunit MurT	-

Subunits

Subunits	Comment	Organism
dimer	1 * 78800, binary complex MurT/GatD, calculated from sequence	Staphylococcus aureus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)