2qm7
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2qm7.jpg|left|200px]] | + | [[Image:2qm7.jpg|left|200px]] |
| - | + | ||
| - | '''MeaB, A Bacterial Homolog of MMAA, Bound to GDP''' | + | {{Structure |
| + | |PDB= 2qm7 |SIZE=350|CAPTION= <scene name='initialview01'>2qm7</scene>, resolution 1.85Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Residue+A+500'>AC1</scene>, <scene name='pdbsite=AC2:Po4+Binding+Site+For+Residue+A+501'>AC2</scene>, <scene name='pdbsite=AC3:Gdp+Binding+Site+For+Residue+A+601'>AC3</scene> and <scene name='pdbsite=AC4:Gdp+Binding+Site+For+Residue+B+602'>AC4</scene> | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= meaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=408 Methylobacterium extorquens]) | ||
| + | }} | ||
| + | |||
| + | '''MeaB, A Bacterial Homolog of MMAA, Bound to GDP''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2QM7 is a [ | + | 2QM7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QM7 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17728257 17728257] |
[[Category: Methylobacterium extorquens]] | [[Category: Methylobacterium extorquens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 26: | Line 35: | ||
[[Category: metallochaperone]] | [[Category: metallochaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:27:14 2008'' |
Revision as of 16:27, 20 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | and | ||||||
| Gene: | meaB (Methylobacterium extorquens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MeaB, A Bacterial Homolog of MMAA, Bound to GDP
Overview
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.
About this Structure
2QM7 is a Single protein structure of sequence from Methylobacterium extorquens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 18:27:14 2008
