This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1rus

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:56, 29 November 2017

CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE

Structural highlights

1rus is a 2 chain structure with sequence from "dicrospirillum_rubrum"_enderlein_1925 "dicrospirillum rubrum" enderlein 1925. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBL2_RHORU] 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. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01339]

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 PubMed

The crystal structure of the binary complex of non-activated ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and its product 3-phospho-D-glycerate has been determined to 2.9-A resolution. This structure determination confirms the proposed location of the active site (Schneider, G., Lindqvist, Y., Branden, C.-I., and Lorimer, G. (1986) EMBO J. 5, 3409-3415) at the carboxyl end of the beta-strands of the alpha/beta-barrel in the carboxyl-terminal domain. One molecule of 3-phosphoglycerate is bound per active site. All oxygen atoms of 3-phosphoglycerate form hydrogen bonds to groups of the enzyme. The phosphate group interacts with the sidechains of residues Arg-288, His-321, and Ser-368, which are conserved between enzymes from different species as well as with the main chain nitrogens from residues Thr-322 and Gly-323. These amino acid residues constitute one of the two phosphate binding sites of the active site. The carboxyl group interacts with the side chains of His-287, Lys-191, and Asn-111. Implications of the activation process for the binding of 3-phosphoglycerate are discussed.

Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate.,Lundqvist T, Schneider G J Biol Chem. 1989 Mar 5;264(7):3643-6. PMID:2492987^[1]

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

References

↑ Lundqvist T, Schneider G. Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate. J Biol Chem. 1989 Mar 5;264(7):3643-6. PMID:2492987

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rus"

Categories: Dicrospirillum rubrum enderlein 1925 | Ribulose-bisphosphate carboxylase | Lundqvist, T | Schneider, G

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE==
 <StructureSection load='1rus' size='340' side='right' caption='[[1rus]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></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='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=1rus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rus OCA], [http://pdbe.org/1rus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rus RCSB], [http://www.ebi.ac.uk/pdbsum/1rus 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=1rus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rus OCA], [http://pdbe.org/1rus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rus RCSB], [http://www.ebi.ac.uk/pdbsum/1rus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rus ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1rus" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[RuBisCO|RuBisCO]]
 == References ==
 <references/>

1rus

From Proteopedia

Revision as of 06:56, 29 November 2017

CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox