5e4y

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'''Unreleased structure'''
 
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The entry 5e4y is ON HOLD
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==Orthorhombic structure of the acetyl esterase MekB==
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<StructureSection load='5e4y' size='340' side='right'caption='[[5e4y]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5e4y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_veronii Pseudomonas veronii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E4Y FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4y OCA], [https://pdbe.org/5e4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e4y RCSB], [https://www.ebi.ac.uk/pdbsum/5e4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q0MRG5_9PSED Q0MRG5_9PSED]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of alpha/beta-hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x-ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl-CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter.
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Authors: Niefind, K., Toelzer, C., Pal, S., Watzlawick, H., Altenbuchner, J.
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A novel esterase subfamily with alpha/beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to l-homoserine O-acetyl transferases.,Tolzer C, Pal S, Watzlawick H, Altenbuchner J, Niefind K FEBS Lett. 2016 Jan;590(1):174-84. doi: 10.1002/1873-3468.12031. Epub 2015 Dec, 28. PMID:26787467<ref>PMID:26787467</ref>
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Description: Orthorhombic structure of the acetyl esterase MekB
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Toelzer, C]]
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<div class="pdbe-citations 5e4y" style="background-color:#fffaf0;"></div>
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[[Category: Altenbuchner, J]]
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== References ==
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[[Category: Pal, S]]
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<references/>
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[[Category: Watzlawick, H]]
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__TOC__
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[[Category: Niefind, K]]
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas veronii]]
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[[Category: Altenbuchner J]]
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[[Category: Niefind K]]
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[[Category: Pal S]]
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[[Category: Toelzer C]]
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[[Category: Watzlawick H]]

Current revision

Orthorhombic structure of the acetyl esterase MekB

PDB ID 5e4y

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