2qm7

<table><tr><td colspan='2'>[[2qm7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metea Metea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QM7 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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">[[2hf8|2hf8]], [[2hf9|2hf9]], [[2qm8|2qm8]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">meaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272630 METEA])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qm7 OCA], [http://pdbe.org/2qm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qm7 RCSB], [http://www.ebi.ac.uk/pdbsum/2qm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qm7 ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

MeaB is an auxiliary protein that plays a crucial role in the protection and assembly of the B(12)-dependent enzyme methylmalonyl-CoA mutase. Impairments in the human homologue of MeaB, MMAA, lead to methylmalonic aciduria, an inborn error of metabolism. To explore the role of this metallochaperone, its structure was solved in the nucleotide-free form, as well as in the presence of product, GDP. MeaB is a homodimer, with each subunit containing a central alpha/beta-core G domain that is typical of the GTPase family, as well as alpha-helical extensions at the N and C termini that are not found in other metalloenzyme chaperone GTPases. The C-terminal extension appears to be essential for nucleotide-independent dimerization, and the N-terminal region is implicated in protein-protein interaction with its partner protein, methylmalonyl-CoA mutase. The structure of MeaB confirms that it is a member of the G3E family of P-loop GTPases, which contains other putative metallochaperones HypB, CooC, and UreG. Interestingly, the so-called switch regions, responsible for signal transduction following GTP hydrolysis, are found at the dimer interface of MeaB instead of being positioned at the surface of the protein where its partner protein methylmalonyl-CoA mutase should bind. This observation suggests a large conformation change of MeaB must occur between the GDP- and GTP-bound forms of this protein. Because of their high sequence homology, the missense mutations in MMAA that result in methylmalonic aciduria have been mapped onto MeaB and, in conjunction with mutagenesis data, provide possible explanations for the pathology of this disease.

Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduria.,Hubbard PA, Padovani D, Labunska T, Mahlstedt SA, Banerjee R, Drennan CL J Biol Chem. 2007 Oct 26;282(43):31308-16. Epub 2007 Aug 28. PMID:17728257<ref>PMID:17728257</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2qm7" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Metea]]

[[Category: Banerjee, R]]

[[Category: Drennan, C L]]

[[Category: Hubbard, P A]]

[[Category: Labunska, T]]

[[Category: Mahlstedt, S A]]

[[Category: Padovani, D]]

[[Category: Metallochaperone]]