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==Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor== | ==Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor== | ||
<StructureSection load='2xk1' size='340' side='right' caption='[[2xk1]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2xk1' size='340' side='right' caption='[[2xk1]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdm|2xdm]], [[1w79|1w79]], [[2wke|2wke]], [[1w8q|1w8q]], [[2vgj|2vgj]], [[1w8y|1w8y]], [[2vgk|2vgk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdm|2xdm]], [[1w79|1w79]], [[2wke|2wke]], [[1w8q|1w8q]], [[2vgj|2vgj]], [[1w8y|1w8y]], [[2vgk|2vgk]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </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=2xk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xk1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xk1 RCSB], [http://www.ebi.ac.uk/pdbsum/2xk1 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=2xk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xk1 OCA], [http://pdbe.org/2xk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xk1 RCSB], [http://www.ebi.ac.uk/pdbsum/2xk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xk1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2xk1" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 15:13, 4 August 2016
Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitorCrystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor
Structural highlights
Function[DAC_ACTSP] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Publication Abstract from PubMedFollowing from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as beta-lactams. Structure guided development of potent reversibly binding penicillin binding protein inhibitors.,Woon EC, Zervosen A, Sauvage E, Simmons KJ, Zivec M, Inglis SR, Fishwick CW, Gobec S, Charlier P, Luxen A, Schofield CJ ACS Med Chem Lett. 2011 Jan 11;2(3):219-23. doi: 10.1021/ml100260x. eCollection, 2011 Mar 10. PMID:24900305[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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