3vcr

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<StructureSection load='3vcr' size='340' side='right'caption='[[3vcr]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='3vcr' size='340' side='right'caption='[[3vcr]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vcr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_14852 Dsm 14852]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3lab 3lab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VCR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vcr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oleispira_antarctica Oleispira antarctica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3lab 3lab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VCR 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=PYR:PYRUVIC+ACID'>PYR</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]] 1.84&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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=3vcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vcr OCA], [https://pdbe.org/3vcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vcr RCSB], [https://www.ebi.ac.uk/pdbsum/3vcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vcr 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=3vcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vcr OCA], [https://pdbe.org/3vcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vcr RCSB], [https://www.ebi.ac.uk/pdbsum/3vcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vcr 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/D2YW47_OLEAN D2YW47_OLEAN]
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Ubiquitous bacteria from the genus Oleispira drive oil degradation in the largest environment on Earth, the cold and deep sea. Here we report the genome sequence of Oleispira antarctica and show that compared with Alcanivorax borkumensis-the paradigm of mesophilic hydrocarbonoclastic bacteria-O. antarctica has a larger genome that has witnessed massive gene-transfer events. We identify an array of alkane monooxygenases, osmoprotectants, siderophores and micronutrient-scavenging pathways. We also show that at low temperatures, the main protein-folding machine Cpn60 functions as a single heptameric barrel that uses larger proteins as substrates compared with the classical double-barrel structure observed at higher temperatures. With 11 protein crystal structures, we further report the largest set of structures from one psychrotolerant organism. The most common structural feature is an increased content of surface-exposed negatively charged residues compared to their mesophilic counterparts. Our findings are relevant in the context of microbial cold-adaptation mechanisms and the development of strategies for oil-spill mitigation in cold environments.
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Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica.,Kube M, Chernikova TN, Al-Ramahi Y, Beloqui A, Lopez-Cortez N, Guazzaroni ME, Heipieper HJ, Klages S, Kotsyurbenko OR, Langer I, Nechitaylo TY, Lunsdorf H, Fernandez M, Juarez S, Ciordia S, Singer A, Kagan O, Egorova O, Alain Petit P, Stogios P, Kim Y, Tchigvintsev A, Flick R, Denaro R, Genovese M, Albar JP, Reva ON, Martinez-Gomariz M, Tran H, Ferrer M, Savchenko A, Yakunin AF, Yakimov MM, Golyshina OV, Reinhardt R, Golyshin PN Nat Commun. 2013 Jul 23;4:2156. doi: 10.1038/ncomms3156. PMID:23877221<ref>PMID:23877221</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 3vcr" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dsm 14852]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Edwards, A M]]
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[[Category: Oleispira antarctica]]
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[[Category: Joachimiak, A]]
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[[Category: Di Leo R]]
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[[Category: Kagan, O]]
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[[Category: Edwards AM]]
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[[Category: Leo, R Di]]
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[[Category: Joachimiak A]]
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[[Category: Structural genomic]]
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[[Category: Kagan O]]
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[[Category: Savchenko, A]]
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[[Category: Savchenko A]]
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[[Category: Stogios, P J]]
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[[Category: Stogios PJ]]
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[[Category: Yim, V]]
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[[Category: Yim V]]
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[[Category: Aldolase superfamily]]
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[[Category: Alpha/beta protein]]
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[[Category: Class i aldolase]]
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[[Category: Kdpg aldolase domain]]
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[[Category: Mcsg]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Tim barrel]]
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[[Category: Tim beta/alpha barrel]]
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[[Category: Unknown function]]
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Current revision

Crystal structure of a putative Kdpg (2-keto-3-deoxy-6-phosphogluconate) aldolase from Oleispira antarctica

PDB ID 3vcr

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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