3lmb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==The crystal structure of the protein OLEI01261 with unknown function from Chlorobaculum tepidum TLS== | ==The crystal structure of the protein OLEI01261 with unknown function from Chlorobaculum tepidum TLS== | ||
<StructureSection load='3lmb' size='340' side='right' caption='[[3lmb]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3lmb' size='340' side='right'caption='[[3lmb]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lmb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oleispira_antarctica_dsm_14852 Oleispira antarctica dsm 14852]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMB OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3lmb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oleispira_antarctica_dsm_14852 Oleispira antarctica dsm 14852]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LMB FirstGlance]. <br> | ||
</td></tr><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> | </td></tr><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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmb OCA], [http://pdbe.org/3lmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lmb RCSB], [http://www.ebi.ac.uk/pdbsum/3lmb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lmb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 30: | Line 30: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Oleispira antarctica dsm 14852]] | [[Category: Oleispira antarctica dsm 14852]] | ||
[[Category: Edwards, A]] | [[Category: Edwards, A]] | ||
Revision as of 10:07, 7 October 2020
The crystal structure of the protein OLEI01261 with unknown function from Chlorobaculum tepidum TLSThe crystal structure of the protein OLEI01261 with unknown function from Chlorobaculum tepidum TLS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUbiquitous 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||