2FG0: Crystal Structure Of A Putative Gamma-d-glutamyl-l-diamino Acid Endopeptidase (npun_r0659) From Nostoc Punctiforme Pcc 73102 At 1.79 A Resolution

Citation:
Abstract
The crystal structures of two homologous endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme were determined at 1.05 and 1.60 A resolution, respectively, and contain a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. The NlpC/P60 domain is a primitive, papain-like peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core. We deduced from structure and sequence analysis, and then experimentally, that these two proteins act as gamma-D-glutamyl-L-diamino acid endopeptidases (EC 3.4.22.-). The active site is located near the interface between the SH3b and NlpC/P60 domains, where the SH3b domain may help define substrate specificity, instead of functioning as a targeting domain, so that only muropeptides with an N-terminal L-alanine can bind to the active site.
PDB ID: 2FG0Download
MMDB ID: 37365
PDB Deposition Date: 2005/12/20
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.79  Å
Source Organism:
Similar Structures:
Biological Unit for 2FG0: dimeric; determined by author and by software (PISA)
Molecular Components in 2FG0
Label Count Molecule
Proteins (2 molecules)
2
Cog0791: Cell Wall-associated Hydrolases (Invasion- Associated Proteins)
Molecule annotation
Chemicals (3 molecules)
1
3
* Click molecule labels to explore molecular sequence information.

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