View source for 2xk1


==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]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xk1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_sp._R39 Actinomadura sp. R39]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2XK1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xk1 OCA], [https://pdbe.org/2xk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xk1 RCSB], [https://www.ebi.ac.uk/pdbsum/2xk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xk1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xk1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinomadura sp. R39]]
[[Category: Large Structures]]
[[Category: Charlier P]]
[[Category: Herman R]]
[[Category: Kerff F]]
[[Category: Rocaboy M]]
[[Category: Sauvage E]]