2z7b

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|PDB= 2z7b |SIZE=350|CAPTION= <scene name='initialview01'>2z7b</scene>, resolution 1.900&Aring;
|PDB= 2z7b |SIZE=350|CAPTION= <scene name='initialview01'>2z7b</scene>, resolution 1.900&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/3-hydroxy-2-methylpyridine-4,5-dicarboxylate_4-decarboxylase 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.51 4.1.1.51]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxy-2-methylpyridine-4,5-dicarboxylate_4-decarboxylase 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.51 4.1.1.51] </span>
|GENE= 5335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381 Mesorhizobium loti])
|GENE= 5335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381 Mesorhizobium loti])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7b OCA], [http://www.ebi.ac.uk/pdbsum/2z7b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2z7b RCSB]</span>
}}
}}
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[[Category: McCulloch, K M.]]
[[Category: McCulloch, K M.]]
[[Category: Mukherjee, T.]]
[[Category: Mukherjee, T.]]
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[[Category: MN]]
 
[[Category: class ii aldolase superfamily]]
[[Category: class ii aldolase superfamily]]
[[Category: lyase]]
[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:52:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:19:12 2008''

Revision as of 02:19, 31 March 2008


PDB ID 2z7b

Drag the structure with the mouse to rotate
, resolution 1.900Å
Ligands: ,
Gene: 5335 (Mesorhizobium loti)
Activity: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase, with EC number 4.1.1.51
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Mesorhizobium loti 3-hydroxy-2-methylpyridine-4,5-dicarboxylate decarboxylase


Overview

The function of the mlr6791 gene from Mesorhizobium loti MAFF303099 has been identified. This gene encodes 3-hydroxy-2-methylpyridine-4,5-dicarboxylate decarboxylase (HMPDdc), an enzyme involved in the catabolism of pyridoxal 5'-phosphate (Vitamin B6). This enzyme was overexpressed in Escherichia coli and characterized. HMPDdc is a 26 kDa protein that catalyzes the decarboxylation of 3-hydroxy-2-methylpyridine-4,5-dicarboxylate to 3-hydroxy-2-methylpyridine-5-carboxylate. The KM and kcat were found to be 366 microM and 0.6 s-1, respectively. The structure of this enzyme was determined at 1.9 A resolution using SAD phasing and belongs to the class II aldolase/adducin superfamily. While the decarboxylation of hydroxy-substituted benzene rings is a common motif in biosynthesis, the mechanism of this reaction is still poorly characterized. The structural studies described here suggest that catalysis of such decarboxylations proceeds by an aldolase-like mechanism.

About this Structure

2Z7B is a Single protein structure of sequence from Mesorhizobium loti. Full crystallographic information is available from OCA.

Reference

Gene identification and structural characterization of the pyridoxal 5'-phosphate degradative protein 3-hydroxy-2-methylpyridine-4,5-dicarboxylate decarboxylase from mesorhizobium loti MAFF303099., Mukherjee T, McCulloch KM, Ealick SE, Begley TP, Biochemistry. 2007 Nov 27;46(47):13606-15. Epub 2007 Oct 31. PMID:17973403

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