2qyg: Difference between revisions
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==Crystal Structure of a RuBisCO-like Protein rlp2 from Rhodopseudomonas palustris== | ==Crystal Structure of a RuBisCO-like Protein rlp2 from Rhodopseudomonas palustris== | ||
<StructureSection load='2qyg' size='340' side='right' caption='[[2qyg]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='2qyg' size='340' side='right'caption='[[2qyg]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qyg]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2qyg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_CGA009 Rhodopseudomonas palustris CGA009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QYG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</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=2qyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qyg OCA], [https://pdbe.org/2qyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qyg RCSB], [https://www.ebi.ac.uk/pdbsum/2qyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qyg ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RBLL2_RHOPA RBLL2_RHOPA] May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/2qyg_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/2qyg_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qyg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2qyg" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Rhodopseudomonas palustris]] | [[Category: Large Structures]] | ||
[[Category: Chan | [[Category: Rhodopseudomonas palustris CGA009]] | ||
[[Category: Eisenberg | [[Category: Chan S]] | ||
[[Category: Li | [[Category: Eisenberg D]] | ||
[[Category: Tabita | [[Category: Li H]] | ||
[[Category: Tabita FR]] | |||
Latest revision as of 14:42, 30 August 2023
Crystal Structure of a RuBisCO-like Protein rlp2 from Rhodopseudomonas palustrisCrystal Structure of a RuBisCO-like Protein rlp2 from Rhodopseudomonas palustris
Structural highlights
FunctionRBLL2_RHOPA May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity (By similarity). 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 PubMedAbout 30 years have now passed since it was discovered that microbes synthesize RubisCO molecules that differ from the typical plant paradigm. RubisCOs of forms I, II, and III catalyze CO(2) fixation reactions, albeit for potentially different physiological purposes, while the RubisCO-like protein (RLP) (form IV RubisCO) has evolved, thus far at least, to catalyze reactions that are important for sulfur metabolism. RubisCO is the major global CO(2) fixation catalyst, and RLP is a somewhat related protein, exemplified by the fact that some of the latter proteins, along with RubisCO, catalyze similar enolization reactions as a part of their respective catalytic mechanisms. RLP in some organisms catalyzes a key reaction of a methionine salvage pathway, while in green sulfur bacteria, RLP plays a role in oxidative thiosulfate metabolism. In many organisms, the function of RLP is unknown. Indeed, there now appear to be at least six different clades of RLP molecules found in nature. Consideration of the many RubisCO (forms I, II, and III) and RLP (form IV) sequences in the database has subsequently led to a coherent picture of how these proteins may have evolved, with a form III RubisCO arising from the Methanomicrobia as the most likely ultimate source of all RubisCO and RLP lineages. In addition, structure-function analyses of RLP and RubisCO have provided information as to how the active sites of these proteins have evolved for their specific functions. Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.,Tabita FR, Hanson TE, Li H, Satagopan S, Singh J, Chan S Microbiol Mol Biol Rev. 2007 Dec;71(4):576-99. PMID:18063718[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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