2xk1
From Proteopedia
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| - | [[ | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xk1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinomadura_sp. Actinomadura sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XK1 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EWB:[(1S)-1-{[(2-BENZYLPHENYL)CARBONYL]AMINO}ETHYL](TRIHYDROXY)BORATE(1-)'>EWB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><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><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><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> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Following 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<ref>PMID:24900305</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
| - | *[[Carboxypeptidase|Carboxypeptidase]] | ||
*[[Penicillin-binding protein|Penicillin-binding protein]] | *[[Penicillin-binding protein|Penicillin-binding protein]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Actinomadura sp.]] | [[Category: Actinomadura sp.]] | ||
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
Revision as of 05:33, 18 June 2014
Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor
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