2iz5: Difference between revisions
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New page: left|200px<br /><applet load="2iz5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2iz5, resolution 2.29Å" /> '''FUNCTION AND STRUCTU... |
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== | ==FUNCTION AND STRUCTURE OF THE MOLYBDENUM COFACTOR CARRIER PROTEIN MCP FROM CHLAMYDOMONAS REINHARDTII== | ||
The molybdenum cofactor (Moco) forms the catalytic site in all eukaryotic | <StructureSection load='2iz5' size='340' side='right'caption='[[2iz5]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2iz5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IZ5 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]] 2.29Å</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=2iz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iz5 OCA], [https://pdbe.org/2iz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iz5 RCSB], [https://www.ebi.ac.uk/pdbsum/2iz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iz5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8RV61_CHLRE Q8RV61_CHLRE] | |||
== 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/iz/2iz5_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=2iz5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The molybdenum cofactor (Moco) forms the catalytic site in all eukaryotic molybdenum enzymes and is synthesized by a multistep biosynthetic pathway. The mechanism of transfer, storage, and insertion of Moco into the appropriate apo-enzyme is poorly understood. In Chlamydomonas reinhardtii, a Moco carrier protein (MCP) has been identified and characterized recently. Here we show biochemical evidence that MCP binds Moco as well as the tungstate-substituted form of the cofactor (Wco) with high affinity, whereas molybdopterin, the ultimate cofactor precursor, is not bound. This binding selectivity points to a specific metal-mediated interaction with MCP, which protects Moco and Wco from oxidation with t((1/2)) of 24 and 96 h, respectively. UV-visible spectroscopy showed defined absorption bands at 393, 470, and 570 nm pointing to ene-diothiolate and protein side-chain charge transfer bonds with molybdenum. We have determined the crystal structure of MCP at 1.6 Angstrom resolution using seleno-methionated and native protein. The monomer constitutes a Rossmann fold with two homodimers forming a symmetrical tetramer in solution. Based on conserved surface residues, charge distribution, shape, in silico docking studies, structural comparisons, and identification of an anionbinding site, a prominent surface depression was proposed as a Moco-binding site, which was confirmed by structure-guided mutagenesis coupled to substrate binding studies. | |||
Function and structure of the molybdenum cofactor carrier protein from Chlamydomonas reinhardtii.,Fischer K, Llamas A, Tejada-Jimenez M, Schrader N, Kuper J, Ataya FS, Galvan A, Mendel RR, Fernandez E, Schwarz G J Biol Chem. 2006 Oct 6;281(40):30186-94. Epub 2006 Jul 27. PMID:16873364<ref>PMID:16873364</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2iz5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fernandez | [[Category: Fernandez E]] | ||
[[Category: Fischer | [[Category: Fischer K]] | ||
[[Category: Kuper | [[Category: Kuper J]] | ||
[[Category: Llamas | [[Category: Llamas A]] | ||
[[Category: Mendel | [[Category: Mendel RR]] | ||
[[Category: Schrader | [[Category: Schrader N]] | ||
[[Category: Schwarz | [[Category: Schwarz G]] | ||
[[Category: Tejada-Jimenez | [[Category: Tejada-Jimenez M]] | ||
Latest revision as of 09:32, 9 May 2024
FUNCTION AND STRUCTURE OF THE MOLYBDENUM COFACTOR CARRIER PROTEIN MCP FROM CHLAMYDOMONAS REINHARDTII
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