1zrs
From Proteopedia
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[[Image:1zrs.gif|left|200px]] | [[Image:1zrs.gif|left|200px]] | ||
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'''wild-type LD-carboxypeptidase''' | '''wild-type LD-carboxypeptidase''' | ||
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[[Category: Bochtler, M.]] | [[Category: Bochtler, M.]] | ||
[[Category: Korza, H J.]] | [[Category: Korza, H J.]] | ||
| - | [[Category: | + | [[Category: Ld-carboxypeptidase]] |
| - | [[Category: | + | [[Category: Nucleophilic elbow]] |
| - | [[Category: | + | [[Category: Peptidoglycan hydrolase]] |
| - | [[Category: | + | [[Category: Serine peptidase]] |
| - | [[Category: | + | [[Category: Serine-histidine-glutamate triad]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:59:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:59, 3 May 2008
wild-type LD-carboxypeptidase
Overview
LD-Carboxypeptidases (EC 3.4.17.13) are named for their ability to cleave amide bonds between l- and d-amino acids, which occur naturally in bacterial peptidoglycan. They are specific for the link between meso-diaminopimelic acid and d-alanine and therefore degrade GlcNAc-MurNAc tetrapeptides to the corresponding tripeptides. As only the tripeptides can be reused as peptidoglycan building blocks, ld-carboxypeptidases are thought to play a role in peptidoglycan recycling. Despite the pharmaceutical interest in peptidoglycan biosynthesis, the fold and catalytic type of ld-carboxypeptidases are unknown. Here, we show that a previously uncharacterized open reading frame in Pseudomonas aeruginosa has ld-carboxypeptidase activity and present the crystal structure of this enzyme. The structure shows that the enzyme consists of an N-terminal beta-sheet and a C-terminal beta-barrel domain. At the interface of the two domains, Ser(115) adopts a highly strained conformation in the context of a strand-turn-helix motif that is similar to the "nucleophilic elbow" in alphabeta-hydrolases. Ser(115) is hydrogen-bonded to a histidine residue, which is oriented by a glutamate residue. All three residues, which occur in the order Ser-Glu-His in the amino acid sequence, are strictly conserved in naturally occurring ld-carboxypeptidases and cannot be mutated to alanines without loss of activity. We conclude that ld-carboxypeptidases are serine peptidases with Ser-His-Glu catalytic triads.
About this Structure
1ZRS is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow., Korza HJ, Bochtler M, J Biol Chem. 2005 Dec 9;280(49):40802-12. Epub 2005 Sep 14. PMID:16162494 Page seeded by OCA on Sat May 3 17:59:32 2008
