3ubm

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<StructureSection load='3ubm' size='340' side='right'caption='[[3ubm]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='3ubm' size='340' side='right'caption='[[3ubm]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ubm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"acetimonas_aceti"_(pasteur_1864)_orla-jensen_1909 "acetimonas aceti" (pasteur 1864) orla-jensen 1909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UBM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ubm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetobacter_aceti Acetobacter aceti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UBM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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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]] 1.992&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uctB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=435 "Acetimonas aceti" (Pasteur 1864) Orla-Jensen 1909])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=3ubm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ubm OCA], [https://pdbe.org/3ubm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ubm RCSB], [https://www.ebi.ac.uk/pdbsum/3ubm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ubm ProSAT]</span></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=3ubm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ubm OCA], [https://pdbe.org/3ubm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ubm RCSB], [https://www.ebi.ac.uk/pdbsum/3ubm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ubm ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A9X6P7_ACEAC A9X6P7_ACEAC]
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Bacterial formyl-CoA:oxalate CoA-transferase (FCOCT) and oxalyl-CoA decarboxylase work in tandem to perform a proton-consuming decarboxylation that has been suggested to have a role in generalized acid resistance. FCOCT is the product of uctB in the acidophilic acetic acid bacterium Acetobacter aceti. As expected for an acid-resistance factor, UctB remains folded at the low pH values encountered in the A. aceti cytoplasm. A comparison of crystal structures of FCOCTs and related proteins revealed few features in UctB that would distinguish it from non-acidophilic proteins and thereby account for its acid stability properties, other than a strikingly featureless electrostatic surface. The apparently neutral surface is a result of a "speckled" charge decoration, in which charged surface residues are surrounded by compensating charges but do not form salt bridges. A quantitative comparison among orthologues identified a pattern of residue substitution in UctB that may be a consequence of selection for protein stability by constant exposure to acetic acid. We suggest that this surface charge pattern, which is a distinctive feature of A. aceti proteins, creates a stabilizing electrostatic network without stiffening the protein or compromising protein-solvent interactions.
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Formyl-coenzyme A (CoA): Oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability.,Mullins EA, Starks CM, Francois JA, Sael L, Kihara D, Kappock TJ Protein Sci. 2012 Feb 28. doi: 10.1002/pro.2054. PMID:22374910<ref>PMID:22374910</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ubm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetobacter aceti]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kappock, T J]]
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[[Category: Kappock TJ]]
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[[Category: Mullins, E A]]
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[[Category: Mullins EA]]
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[[Category: Starks, C M]]
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[[Category: Starks CM]]
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[[Category: Transferase]]
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Current revision

Formyl-CoA:oxalate CoA-transferase from Acetobacter aceti

PDB ID 3ubm

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