5z03

From Proteopedia

(Difference between revisions)

Revision as of 08:27, 2 May 2018

Mutant (S106A) Escherichia coli L,D-carboxypeptidase A (LdcA)

Structural highlights

5z03 is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ldcA, ycgQ, b1192, JW1181 (ECOLI)
Activity:	Muramoyltetrapeptide carboxypeptidase, with EC number 3.4.17.13
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Templin MF, Ursinus A, Holtje JV. A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. EMBO J. 1999 Aug 2;18(15):4108-17. doi: 10.1093/emboj/18.15.4108. PMID:10428950 doi:http://dx.doi.org/10.1093/emboj/18.15.4108
↑ Park JT, Uehara T. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol Mol Biol Rev. 2008 Jun;72(2):211-27, table of contents. doi:, 10.1128/MMBR.00027-07. PMID:18535144 doi:http://dx.doi.org/10.1128/MMBR.00027-07
↑ Meyer K, Addy C, Akashi S, Roper DI, Tame JRH. The crystal structure and oligomeric form of Escherichia colil,d-carboxypeptidase A. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2018.03.195

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5z03"

@@ Line 3: / Line 3: @@
 <StructureSection load='5z03' size='340' side='right' caption='[[5z03]], [[Resolution|resolution]] 1.75&Aring;' 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>
+<table><tr><td colspan='2'>[[5z03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ldcA, ycgQ, b1192, JW1181 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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>
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Ecoli]]
 [[Category: Muramoyltetrapeptide carboxypeptidase]]
 [[Category: Meyer, K]]

5z03

From Proteopedia

Revision as of 08:27, 2 May 2018

Mutant (S106A) Escherichia coli L,D-carboxypeptidase A (LdcA)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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