3rg6

From Proteopedia

(Difference between revisions)

Revision as of 06:02, 15 June 2022

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco

Structural highlights

3rg6 is a 6 chain structure with sequence from Anabaena sp. and Anacystis nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2wvw, 3hyb, 2peo, 1rbl
Gene:	cbbL, rbcA, rbcL, syc0130_c (Anacystis nidulans), rbcX (Anabaena sp.)
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBL_SYNP6] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]

Publication Abstract from PubMed

The form I Rubisco of autotrophic bacteria, algae and plants is a complex of eight large (RbcL) and eight small (RbcS) subunits. It fixes atmospheric CO(2) in the dark reaction of photosynthesis. As shown for the cyanobacterial enzyme, folding of the RbcL subunits is mediated by the GroEL-GroES chaperonin system, and assembly requires the specialized chaperone RbcX, a homodimer of ~15-kDa subunits. Here we present the 3.2-A crystal structure of a Rubisco assembly intermediate, consisting of the RbcL(8) core with eight RbcX(2) molecules bound. The structure reveals the molecular mechanism by which RbcX(2) mediates oligomeric assembly. Specifically, RbcX(2) provides positional information for proper formation of antiparallel RbcL dimers, thereby preventing RbcL-RbcL misalignment and off-pathway aggregation. The RbcL(8)(RbcX(2))(8) structure also suggests that RbcS functions by stabilizing the '60s loop' of RbcL in the catalytically active conformation.

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.,Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M Nat Struct Mol Biol. 2011 Jul 17. doi: 10.1038/nsmb.2090. PMID:21765418^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M. Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nat Struct Mol Biol. 2011 Jul 17. doi: 10.1038/nsmb.2090. PMID:21765418 doi:10.1038/nsmb.2090

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3rg6"

@@ Line 3: / Line 3: @@
 <StructureSection load='3rg6' size='340' side='right'caption='[[3rg6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3rg6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] and [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RG6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3rg6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] and [https://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RG6 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wvw|2wvw]], [[3hyb|3hyb]], [[2peo|2peo]], [[1rbl|1rbl]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wvw|2wvw]], [[3hyb|3hyb]], [[2peo|2peo]], [[1rbl|1rbl]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbL, rbcA, rbcL, syc0130_c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269084 Anacystis nidulans]), rbcX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbL, rbcA, rbcL, syc0130_c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269084 Anacystis nidulans]), rbcX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=3rg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg6 OCA], [http://pdbe.org/3rg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rg6 RCSB], [http://www.ebi.ac.uk/pdbsum/3rg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rg6 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=3rg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg6 OCA], [https://pdbe.org/3rg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rg6 RCSB], [https://www.ebi.ac.uk/pdbsum/3rg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rg6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
+[[https://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 ==See Also==
-*[[RuBisCO|RuBisCO]]
+*[[RuBisCO 3D structures|RuBisCO 3D structures]]
 == References ==
 <references/>

3rg6

From Proteopedia

Revision as of 06:02, 15 June 2022

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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