2z7b: Difference between revisions
New page: left|200px<br /><applet load="2z7b" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z7b, resolution 1.900Å" /> '''Crystal Structure o... |
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==Overview== | ==Overview== | ||
The function of the mlr6791 gene from Mesorhizobium loti MAFF303099 has | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
Gene | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17973403 17973403] | ||
[[Category: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase]] | [[Category: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase]] | ||
[[Category: Mesorhizobium loti]] | [[Category: Mesorhizobium loti]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Begley, T | [[Category: Begley, T P.]] | ||
[[Category: Ealick, S | [[Category: Ealick, S E.]] | ||
[[Category: McCulloch, K | [[Category: McCulloch, K M.]] | ||
[[Category: Mukherjee, T.]] | [[Category: Mukherjee, T.]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:40 2008'' | ||
Revision as of 17:00, 21 February 2008
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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 with MN as ligand. Active as 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase, with EC number 4.1.1.51 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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