View source for 1iwa


==RUBISCO FROM GALDIERIA PARTITA==
<StructureSection load='1iwa' size='340' side='right'caption='[[1iwa]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iwa]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IWA 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1iwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwa OCA], [https://pdbe.org/1iwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iwa RCSB], [https://www.ebi.ac.uk/pdbsum/1iwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O98949_9RHOD O98949_9RHOD] 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 (By similarity).[HAMAP-Rule:MF_01338]
== 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/iw/1iwa_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=1iwa ConSurf].
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== Publication Abstract from PubMed ==
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the reactions of carboxylation and oxygenation of ribulose-1,5-bisphosphate. These reactions require that the active site should be closed by a flexible loop (loop 6) of the large subunit. Rubisco from a red alga, Galdieria partita, has the highest specificity for carboxylation reaction among the Rubiscos hitherto reported. The crystal structure of unactivated Galdieria Rubisco has been determined at 2.6 A resolution. The electron density map reveals that a sulfate binds only to the P1 anion-binding site of the active site and the loop 6 is closed. Galdieria Rubisco has a unique hydrogen bond between the main chain oxygen of Val332 on the loop 6 and the epsilon-amino group of Gln386 of the same large subunit. This interaction is likely to be crucial to understanding for stabilizing the loop 6 in the closed state and to making a higher affinity for anionic ligands.

X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site.,Okano Y, Mizohata E, Xie Y, Matsumura H, Sugawara H, Inoue T, Yokota A, Kai Y FEBS Lett. 2002 Sep 11;527(1-3):33-6. PMID:12220629<ref>PMID:12220629</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1iwa" style="background-color:#fffaf0;"></div>

==See Also==
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Galdieria partita]]
[[Category: Large Structures]]
[[Category: Inoue T]]
[[Category: Kai Y]]
[[Category: Matsumura H]]
[[Category: Mizohata E]]
[[Category: Okano Y]]
[[Category: Sugawara H]]
[[Category: Xie Y]]
[[Category: Yokota A]]