5z03
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Mutant (S106A) Escherichia coli L,D-carboxypeptidase A (LdcA)== | |
| + | <StructureSection load='5z03' size='340' side='right' caption='[[5z03]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5z03]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z03 FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Muramoyltetrapeptide_carboxypeptidase Muramoyltetrapeptide carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.13 3.4.17.13] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z03 OCA], [http://pdbe.org/5z03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z03 RCSB], [http://www.ebi.ac.uk/pdbsum/5z03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z03 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LDCA_ECOLI LDCA_ECOLI]] Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase.<ref>PMID:10428950</ref> <ref>PMID:18535144</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial peptidoglycan is constructed by cross-linking sugar chains carrying pentapeptide building blocks with two d-alanine residues at the C-terminus. Incorporation into the polymer and subsequent breakdown of peptidoglycan releases a tetrapeptide with a single d-alanine residue. Removal of this residue is necessary for the tripeptide to receive a new D-Ala-D-Ala dipeptide in the synthetic pathway, but proteases are generally unable to work with substrates having residues of unusual chirality close to the scissile bond. Processing of the tetrapeptide is carried out by a dedicated ld-carboxypeptidase, which is of interest as a novel drug target. We describe the high resolution crystal structure of the enzyme from E. coli, and demonstrate the dimeric structure is highly conserved. | ||
| - | + | The crystal structure and oligomeric form of Escherichia colil,d-carboxypeptidase A.,Meyer K, Addy C, Akashi S, Roper DI, Tame JRH Biochem Biophys Res Commun. 2018 May 15;499(3):594-599. doi:, 10.1016/j.bbrc.2018.03.195. Epub 2018 Apr 5. PMID:29601819<ref>PMID:29601819</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5z03" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Muramoyltetrapeptide carboxypeptidase]] | ||
[[Category: Meyer, K]] | [[Category: Meyer, K]] | ||
| + | [[Category: Tame, J R.H]] | ||
| + | [[Category: Cell-wall]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Peptidoglycan]] | ||
| + | [[Category: Recycling]] | ||
Revision as of 05:30, 25 April 2018
Mutant (S106A) Escherichia coli L,D-carboxypeptidase A (LdcA)
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