2hbv
From Proteopedia
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|PDB= 2hbv |SIZE=350|CAPTION= <scene name='initialview01'>2hbv</scene>, resolution 1.650Å | |PDB= 2hbv |SIZE=350|CAPTION= <scene name='initialview01'>2hbv</scene>, resolution 1.650Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aminocarboxymuconate-semialdehyde_decarboxylase Aminocarboxymuconate-semialdehyde decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.45 4.1.1.45] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminocarboxymuconate-semialdehyde_decarboxylase Aminocarboxymuconate-semialdehyde decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.45 4.1.1.45] </span> |
|GENE= nbaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 Pseudomonas fluorescens]) | |GENE= nbaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 Pseudomonas fluorescens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2hbx|2HBX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hbv OCA], [http://www.ebi.ac.uk/pdbsum/2hbv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hbv RCSB]</span> | ||
}} | }} | ||
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[[Category: Yang, K.]] | [[Category: Yang, K.]] | ||
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: ZN]] | ||
[[Category: acmsd]] | [[Category: acmsd]] | ||
[[Category: decarboxylase]] | [[Category: decarboxylase]] | ||
| Line 36: | Line 37: | ||
[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:28:16 2008'' |
Revision as of 00:28, 31 March 2008
| |||||||
| , resolution 1.650Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | nbaD (Pseudomonas fluorescens) | ||||||
| Activity: | Aminocarboxymuconate-semialdehyde decarboxylase, with EC number 4.1.1.45 | ||||||
| Related: | 2HBX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde-Decarboxylase (ACMSD)
Overview
Alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) is a widespread enzyme found in many bacterial species and all currently sequenced eukaryotic organisms. It occupies a key position at the branching point of two metabolic pathways: the tryptophan to quinolinate pathway and the bacterial 2-nitrobenzoic acid degradation pathway. The activity of ACMSD determines whether the metabolites in both pathways are converted to quinolinic acid for NAD biosynthesis or to acetyl-CoA for the citric acid cycle. Here we report the first high-resolution crystal structure of ACMSD from Pseudomonas fluorescens which validates our previous predictions that this enzyme is a member of the metal-dependent amidohydrolase superfamily of the (beta/alpha)(8) TIM barrel fold. The structure of the enzyme in its native form, determined at 1.65 A resolution, reveals the precise spatial arrangement of the active site metal center and identifies a potential substrate-binding pocket. The identity of the native active site metal was determined to be Zn. Also determined was the structure of the enzyme complexed with cobalt at 2.50 A resolution. The hydrogen bonding network around the metal center suggests that Arg51 and His228 may play important roles in catalysis. The metal center configuration of PfACMSD is very similar to that of Zn-dependent adenosine deaminase and Fe-dependent cytosine deaminase, suggesting that ACMSD may share certain similarities in its catalytic mechanism with these enzymes. These data enable us to propose possible catalytic mechanisms for ACMSD which appear to be unprecedented among all currently characterized decarboxylases.
About this Structure
2HBV is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
Crystal structure of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase: insight into the active site and catalytic mechanism of a novel decarboxylation reaction., Martynowski D, Eyobo Y, Li T, Yang K, Liu A, Zhang H, Biochemistry. 2006 Sep 5;45(35):10412-21. PMID:16939194
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