4p6b: Difference between revisions
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New page: '''Unreleased structure''' The entry 4p6b is ON HOLD Authors: Ngo, T.D., Ryu, B.H., Ju, H.S., Jang, E.J., Kim, K.K., Kim, D.H. Description: Crystal structure of Est-Y29,a novel penicil... |
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==Crystal structure of Est-Y29,a novel penicillin-binding protein/beta-lactamase homolog from a metagenomic library== | |||
<StructureSection load='4p6b' size='340' side='right'caption='[[4p6b]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4p6b]] 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=4P6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P6B 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]] 1.7Å</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=4p6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6b OCA], [https://pdbe.org/4p6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p6b RCSB], [https://www.ebi.ac.uk/pdbsum/4p6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6b 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4p6b" 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]] | |||
Latest revision as of 00:40, 28 December 2023
Crystal structure of Est-Y29,a novel penicillin-binding protein/beta-lactamase homolog from a metagenomic library
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