2aun: Difference between revisions

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[[Image:2aun.gif|left|200px]]
{{Seed}}
[[Image:2aun.png|left|200px]]


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{{STRUCTURE_2aun|  PDB=2aun  |  SCENE=  }}  
{{STRUCTURE_2aun|  PDB=2aun  |  SCENE=  }}  


'''Active site His285Ala mutant of LD-carboxypeptidase'''
===Active site His285Ala mutant of LD-carboxypeptidase===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16162494}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16162494 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16162494}}


==About this Structure==
==About this Structure==
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[[Category: Serine peptidase]]
[[Category: Serine peptidase]]
[[Category: Serine-histidine-glutamate triad]]
[[Category: Serine-histidine-glutamate triad]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:29:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:54:04 2008''

Revision as of 09:54, 28 July 2008

File:2aun.png

Template:STRUCTURE 2aun

Active site His285Ala mutant of LD-carboxypeptidase

Template:ABSTRACT PUBMED 16162494

About this Structure

2AUN 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

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