1b1a
From Proteopedia
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| - | [[Image:1b1a.gif|left|200px]] | + | [[Image:1b1a.gif|left|200px]] |
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| - | '''GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1b1a |SIZE=350|CAPTION= <scene name='initialview01'>1b1a</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methylaspartate_mutase Methylaspartate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.1 5.4.99.1] | ||
| + | |GENE= GLMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1494 Clostridium cochlearium]) | ||
| + | }} | ||
| + | |||
| + | '''GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B1A is a [ | + | 1B1A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1A OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium., Hoffmann B, Konrat R, Bothe H, Buckel W, Krautler B, Eur J Biochem. 1999 Jul;263(1):178-88. PMID:[http:// | + | Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium., Hoffmann B, Konrat R, Bothe H, Buckel W, Krautler B, Eur J Biochem. 1999 Jul;263(1):178-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10429202 10429202] |
[[Category: Clostridium cochlearium]] | [[Category: Clostridium cochlearium]] | ||
[[Category: Methylaspartate mutase]] | [[Category: Methylaspartate mutase]] | ||
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[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''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 10:05:06 2008'' |
Revision as of 08:05, 20 March 2008
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| Gene: | GLMS (Clostridium cochlearium) | ||||||
| Activity: | Methylaspartate mutase, with EC number 5.4.99.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE
Overview
Glutamate mutase (Glm) is an adenosylcobamide-dependent enzyme that catalyzes the reversible rearrangement of (2S)-glutamate to (2S, 3S)-3-methylaspartate. The active enzyme from Clostridium cochlearium consists of two subunits (of 53.6 and 14.8 kDa) as an alpha2beta2 tetramer, whose assembly is mediated by coenzyme B12. The smaller of the protein components, GlmS, has been suggested to be the B12-binding subunit. Here we report the solution structure of GlmS, determined from a heteronuclear NMR-study, and the analysis of important dynamical aspects of this apoenzyme subunit. The global fold and dynamic behavior of GlmS in solution are similar to those of the corresponding subunit MutS from C. tetanomorphum, which has previously been investigated using NMR-spectroscopy. Both solution structures of the two Glm B12-binding subunits share striking similarities with that determined by crystallography for the B12-binding domain of methylmalonyl CoA mutase (Mcm) from Propionibacterium shermanii, which is B12 bound. In the crystal structure a conserved histidine residue was found to be coordinated to cobalt, displacing the endogenous axial ligand of the cobamide. However, in GlmS and MutS the sequence motif, Asp-x-His-x-x-Gly, which includes the cobalt-coordinating histidine residue, and a predicted alpha-helical region following the motif, are present as an unstructured and highly mobile loop. In the absence of coenzyme, the B12-binding site apparently is only partially formed. By comparing the crystal structure of Mcm with the solution structures of B12-free GlmS and MutS, a consistent picture on the mechanism of B12 binding has been obtained. Important elements of the binding site only become structured upon binding B12; these include the cobalt-coordinating histidine residue, and an alpha helix that forms one side of the cleft accommodating the nucleotide 'tail' of the coenzyme.
About this Structure
1B1A is a Single protein structure of sequence from Clostridium cochlearium. Full crystallographic information is available from OCA.
Reference
Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium., Hoffmann B, Konrat R, Bothe H, Buckel W, Krautler B, Eur J Biochem. 1999 Jul;263(1):178-88. PMID:10429202
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