1rus: Difference between revisions

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New page: left|200px<br /><applet load="1rus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rus, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1rus.gif|left|200px]]<br /><applet load="1rus" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rus, resolution 2.9&Aring;" />
'''CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE==
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.
<StructureSection load='1rus' size='340' side='right'caption='[[1rus]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></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=1rus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rus OCA], [https://pdbe.org/1rus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rus RCSB], [https://www.ebi.ac.uk/pdbsum/1rus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rus ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBL2_RHORU 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ru/1rus_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1rus ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with 3PG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RUS OCA].
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2492987 2492987]
[[Category: Large Structures]]
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Lundqvist T]]
[[Category: Single protein]]
[[Category: Schneider G]]
[[Category: Lundqvist, T.]]
[[Category: Schneider, G.]]
[[Category: 3PG]]
[[Category: lyase(carbon-carbon)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:52:55 2007''

Latest revision as of 11:26, 14 February 2024

CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATECRYSTAL 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 Rhodospirillum rubrum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:
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.

See Also

1rus, resolution 2.90Å

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