View source for 4p85


==Crystal structure of Est-Y29, a novel penicillin-binding protein/beta-lactamase homolog from a metagenomic library==
<StructureSection load='4p85' size='340' side='right'caption='[[4p85]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4p85]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Metagenome Metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P85 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</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=4p85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p85 OCA], [https://pdbe.org/4p85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p85 RCSB], [https://www.ebi.ac.uk/pdbsum/4p85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p85 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interest in penicillin-binding proteins and beta-lactamases (the PBP-betaL family) is increasing owing to their biological and clinical significance. In this study, the crystal structure of Est-Y29, a metagenomic homologue of the PBP-betaL family, was determined at 1.7 A resolution. In addition, complex structures of Est-Y29 with 4-nitrophenyl phosphate (4NP) and with diethyl phosphonate (DEP) at 2.0 A resolution were also elucidated. Structural analyses showed that Est-Y29 is composed of two domains: a beta-lactamase fold and an insertion domain. A deep hydrophobic patch between these domains defines a wide active site, and a nucleophilic serine (Ser58) residue is located in a groove defined primarily by hydrophobic residues between the two domains. In addition, three hydrophobic motifs, which make up the substrate-binding site, allow this enzyme to hydrolyze a wide variety of hydrophobic compounds, including fish and olive oils. Furthermore, cross-linked Est-Y29 aggregates (CLEA-Est-Y29) significantly increase the stability of the enzyme as well as its potential for extensive reuse in various deactivating conditions. The structural features of Est-Y29, together with biochemical and biophysical studies, could provide a molecular basis for understanding the properties and regulatory mechanisms of the PBP-betaL family and their potential for use in industrial biocatalysts.

Crystallographic analysis and biochemical applications of a novel penicillin-binding protein/beta-lactamase homologue from a metagenomic library.,Ngo TD, Ryu BH, Ju H, Jang EJ, Kim KK, Kim TD Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2455-66. doi:, 10.1107/S1399004714015272. Epub 2014 Aug 29. PMID:25195758<ref>PMID:25195758</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4p85" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Metagenome]]
[[Category: Jang EJ]]
[[Category: Ju HS]]
[[Category: Kim DH]]
[[Category: Kim KK]]
[[Category: Ngo TD]]
[[Category: Ryu BH]]