1e4e

From Proteopedia

(Difference between revisions)

Revision as of 05:38, 6 October 2017

D-alanyl-D-lacate ligase

Structural highlights

1e4e is a 2 chain structure with sequence from Atcc 19434. The December 2015 RCSB PDB Molecule of the Month feature on Vancomycin by David Goodsell is 10.2210/rcsb_pdb/mom_2015_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1iow, 1iov
Gene:	VANA (ATCC 19434)
Activity:	D-alanine--(R)-lactate ligase, with EC number 6.1.2.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VANA_ENTFC] Required for high-level resistance to glycopeptide antibiotics. D-Ala--D-Ala ligase of altered specificity which catalyzes ester bond formation between D-Ala and various D-hydroxy acids; produces a peptidoglycan which does not terminate in D-alanine but in D-lactate, thus preventing vancomycin or teicoplanin binding.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

d-alanine-d-lactate ligase from Enterococcus faecium BM4147 is directly responsible for the biosynthesis of alternate cell-wall precursors in bacteria, which are resistant to the glycopeptide antibiotic vancomycin. The crystal structure has been determined with data extending to 2.5-A resolution. This structure shows that the active site has unexpected interactions and is distinct from previous models for d-alanyl-d-lactate ligase mechanistic studies. It appears that the preference of the enzyme for lactate as a ligand over d-alanine could be mediated by electrostatic effects and/or a hydrogen-bonding network, which principally involve His-244. The structure of d-alanyl-d-lactate ligase provides a revised interpretation of the molecular events that lead to vancomycin resistance.

The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA).,Roper DI, Huyton T, Vagin A, Dodson G Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8921-5. PMID:10908650^[2]

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

References

↑ Bugg TD, Wright GD, Dutka-Malen S, Arthur M, Courvalin P, Walsh CT. Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry. 1991 Oct 29;30(43):10408-15. PMID:1931965
↑ Roper DI, Huyton T, Vagin A, Dodson G. The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA). Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8921-5. PMID:10908650 doi:http://dx.doi.org/10.1073/pnas.150116497

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e4e"

@@ Line 1: / Line 1: @@
-==D-ALANYL-D-LACATE LIGASE==
+==D-alanyl-D-lacate ligase==
 <StructureSection load='1e4e' size='340' side='right' caption='[[1e4e]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VANA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 ATCC 19434])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-alanine--(R)-lactate_ligase D-alanine--(R)-lactate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.2.1 6.1.2.1] </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=1e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4e OCA], [http://pdbe.org/1e4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e4e RCSB], [http://www.ebi.ac.uk/pdbsum/1e4e PDBsum]</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=1e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4e OCA], [http://pdbe.org/1e4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e4e RCSB], [http://www.ebi.ac.uk/pdbsum/1e4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4e ProSAT]</span></td></tr>
 </table>
 == Function ==

1e4e

From Proteopedia

Revision as of 05:38, 6 October 2017

D-alanyl-D-lacate ligase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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