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| | {{STRUCTURE_1b1a| PDB=1b1a | SCENE= }} | | {{STRUCTURE_1b1a| PDB=1b1a | SCENE= }} |
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| - | '''GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE'''
| + | ===GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10429202}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10429202 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10429202}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 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]. | + | 1B1A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1A OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Glutamate mutase]] | | [[Category: Glutamate mutase]] |
| | [[Category: Isomerase]] | | [[Category: Isomerase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:57:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:02:18 2008'' |
Revision as of 15:02, 30 June 2008
Template:STRUCTURE 1b1a
GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE
Template:ABSTRACT PUBMED 10429202
About this Structure
1B1A is a Single protein structure of sequence from Clostridium cochlearium. Full experimental 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
Page seeded by OCA on Mon Jun 30 18:02:18 2008
