2pei: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pei]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp._pcc_7002 Synechococcus sp. pcc 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PEI FirstGlance]. <br> | <table><tr><td colspan='2'>[[2pei]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp._pcc_7002 Synechococcus sp. pcc 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PEI FirstGlance]. <br> | ||
</td></tr><tr><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pej|2pej]], [[2pek|2pek]], [[2pem|2pem]], [[2pen|2pen]], [[2peo|2peo]], [[2peq|2peq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pej|2pej]], [[2pek|2pek]], [[2pem|2pem]], [[2pen|2pen]], [[2peo|2peo]], [[2peq|2peq]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RbcX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Synechococcus sp. PCC 7002])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RbcX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Synechococcus sp. PCC 7002])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pei RCSB], [http://www.ebi.ac.uk/pdbsum/2pei PDBsum]</span></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=2pei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pei RCSB], [http://www.ebi.ac.uk/pdbsum/2pei PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Synechococcus sp. pcc 7002]] | [[Category: Synechococcus sp. pcc 7002]] | ||
[[Category: Bracher, A | [[Category: Bracher, A]] | ||
[[Category: Hartl, F U | [[Category: Hartl, F U]] | ||
[[Category: Hayer-Hartl, M | [[Category: Hayer-Hartl, M]] | ||
[[Category: Rao, B Vasudeva | [[Category: Rao, B Vasudeva]] | ||
[[Category: Rao, K Vasudeva | [[Category: Rao, K Vasudeva]] | ||
[[Category: Saschenbrecker, S | [[Category: Saschenbrecker, S]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Helix bundle]] | [[Category: Helix bundle]] | ||
[[Category: Protein complex assembly]] | [[Category: Protein complex assembly]] | ||
Revision as of 18:13, 19 January 2015
Crystal structure of selenomethionine-labeled RbcXCrystal structure of selenomethionine-labeled RbcX
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 PubMedAfter folding, many proteins must assemble into oligomeric complexes to become biologically active. Here we describe the role of RbcX as an assembly chaperone of ribulose-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme responsible for the fixation of atmospheric carbon dioxide. In cyanobacteria and plants, Rubisco is an approximately 520 kDa complex composed of eight large subunits (RbcL) and eight small subunits (RbcS). We found that cyanobacterial RbcX functions downstream of chaperonin-mediated RbcL folding in promoting the formation of RbcL(8) core complexes. Structural analysis revealed that the 15 kDa RbcX forms a homodimer with two cooperating RbcL-binding regions. A central cleft specifically binds the exposed C-terminal peptide of RbcL subunits, enabling a peripheral surface of RbcX to mediate RbcL(8) assembly. Due to the dynamic nature of these interactions, RbcX is readily displaced from RbcL(8) complexes by RbcS, producing the active enzyme. The strategies employed by RbcX in achieving substrate specificity and efficient product release may be generally relevant in assisted assembly reactions. Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco.,Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M Cell. 2007 Jun 15;129(6):1189-200. PMID:17574029[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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