View source for 6y01


==The structure of the molybdenum cofactor binding protein from the phototrophic bacterium Rippkaea orientalis==
<StructureSection load='6y01' size='340' side='right'caption='[[6y01]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6y01]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rippkaea_orientalis_PCC_8801 Rippkaea orientalis PCC 8801]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y01 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]] 1.23&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=6y01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y01 OCA], [https://pdbe.org/6y01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y01 RCSB], [https://www.ebi.ac.uk/pdbsum/6y01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y01 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7K4Z0_RIPO1 B7K4Z0_RIPO1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The molybdenum cofactor (Moco) is the prosthetic group of all molybdenum-dependent enzymes except for nitrogenase. The multistep biosynthesis pathway of Moco and its function in molybdenum-dependent enzymes are already well understood. The mechanisms of Moco transfer, storage and insertion, on the other hand, are not. In the cell, Moco is usually not found in its free form and remains bound to proteins because of its sensitivity to oxidation. The green alga Chlamydomonas reinhardtii harbors a Moco carrier protein (MCP) that binds and protects Moco but is devoid of enzymatic function. It has been speculated that this MCP acts as a means of Moco storage and transport. Here, the search for potential MCPs has been extended to the prokaryotes, and many MCPs were found in cyanobacteria. A putative MCP from Rippkaea orientalis (RoMCP) was selected for recombinant production, crystallization and structure determination. RoMCP has a Rossmann-fold topology that is characteristic of nucleotide-binding proteins and a homotetrameric quaternary structure similar to that of the MCP from C. reinhardtii. In each protomer, a positively charged crevice was identified that accommodates up to three chloride ions, hinting at a potential Moco-binding site. Computational docking experiments supported this notion and gave an impression of the RoMCP-Moco complex.

The structure of the Moco carrier protein from Rippkaea orientalis.,Krausze J, Hercher TW, Archna A, Kruse T Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):453-463. doi:, 10.1107/S2053230X20011073. Epub 2020 Aug 28. PMID:32880594<ref>PMID:32880594</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6y01" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rippkaea orientalis PCC 8801]]
[[Category: Krausze J]]