1h9j

<table><tr><td colspan='2'>[[1h9j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1H9J FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1atg|1atg]], [[1h9k|1h9k]], [[1h9m|1h9m]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MODG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 ATCC 478])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1h9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9j OCA], [http://pdbe.org/1h9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h9j RCSB], [http://www.ebi.ac.uk/pdbsum/1h9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h9j ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The X-ray structures of the cytoplasmic molybdate-binding protein ModG from Azotobacter vinelandii in two different crystal forms have been determined. For such a small protein it is remarkably complex. Each 14.3 kDa subunit contains two small beta-barrel domains, which display an OB-fold motif, also seen in the related structure of ModE, a molybdenum-dependent transcriptional regulator, and very recently in the Mop protein that, like ModG, has been implicated in molybdenum homeostasis within the cell. In contrast to earlier speculation, the functional unit of ModG is actually not a dimer (as in ModE), but a trimer capable of binding a total of eight molybdate molecules that are distributed between two disparate types of site. All the binding sites are located at subunit interfaces, with one type lying on a crystallographic 3-fold axis, whilst the other lies between pairs of subunits. The two types of site are linked by short hydrogen bond networks that may suggest a cooperative binding mechanism. A superposition of two subunits of the ModG trimer on the apo-ModE dimer allows the probable locations of the molybdate-binding sites of the latter to be assigned. Through structural comparisons with other oxyanion-binding proteins, including Mop and ModE, it is possible to speculate about ligand-binding affinities, selectivity and evolution. Copyright 12001 Academic Press.

Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity.,Delarbre L, Stevenson CE, White DJ, Mitchenall LA, Pau RN, Lawson DM J Mol Biol. 2001 May 18;308(5):1063-79. PMID:11352591<ref>PMID:11352591</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 1h9j" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 478]]

[[Category: Delarbre, L]]

[[Category: Lawson, D M]]

[[Category: Mitchenall, L A]]

[[Category: Pau, R N]]

[[Category: Stevenson, C E.M]]

[[Category: White, D J]]

[[Category: Molybdate homeostasis]]