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| | <StructureSection load='5d7b' size='340' side='right'caption='[[5d7b]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='5d7b' size='340' side='right'caption='[[5d7b]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d7b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D7B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d7b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D7B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d60|5d60]]</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=5d7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7b OCA], [https://pdbe.org/5d7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d7b RCSB], [https://www.ebi.ac.uk/pdbsum/5d7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7b ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cg0961, Cgl0839 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7b OCA], [http://pdbe.org/5d7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d7b RCSB], [http://www.ebi.ac.uk/pdbsum/5d7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8NS43_CORGL Q8NS43_CORGL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcus glutamicus kinoshita et al. 1958]] | + | [[Category: Corynebacterium glutamicum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altenbuchner, J]] | + | [[Category: Altenbuchner J]] |
| - | [[Category: Niefind, K]] | + | [[Category: Niefind K]] |
| - | [[Category: Pal, S]] | + | [[Category: Pal S]] |
| - | [[Category: Toelzer, C]] | + | [[Category: Toelzer C]] |
| - | [[Category: Watzlawick, H]] | + | [[Category: Watzlawick H]] |
| - | [[Category: Acetylester hydrolase]]
| + | |
| - | [[Category: Alpha/beta-hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q8NS43_CORGL
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tolzer C, Pal S, Watzlawick H, Altenbuchner J, Niefind K. A novel esterase subfamily with alpha/beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to l-homoserine O-acetyl transferases. FEBS Lett. 2016 Jan;590(1):174-84. doi: 10.1002/1873-3468.12031. Epub 2015 Dec, 28. PMID:26787467 doi:http://dx.doi.org/10.1002/1873-3468.12031
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