1uwl
From Proteopedia
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|SITE= <scene name='pdbsite=AC1:Nad+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Nad+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Urocanate_hydratase Urocanate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.49 4.2.1.49] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Urocanate_hydratase Urocanate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.49 4.2.1.49] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwl OCA], [http://www.ebi.ac.uk/pdbsum/1uwl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uwl RCSB]</span> | ||
}} | }} | ||
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[[Category: Retey, J.]] | [[Category: Retey, J.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: NAD]] | ||
[[Category: histidine metabolism]] | [[Category: histidine metabolism]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: urocanase]] | [[Category: urocanase]] | ||
| - | ''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 00:16:17 2008'' |
Revision as of 21:16, 30 March 2008
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| , resolution 1.76Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Urocanate hydratase, with EC number 4.2.1.49 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.76A STRUCTURE OF UROCANATE HYDRATASE FROM PSEUDOMONAS PUTIDA
Overview
Urocanase (EC 4.2.1.49) from Pseudomonas putida was crystallized after removing one of the seven free thiol groups. The crystal structure was solved by multiwavelength anomalous diffraction (MAD) using a seleno-methionine derivative and then refined at 1.14 A resolution. The enzyme is a symmetric homodimer of 2 x 557 amino acid residues with tightly bound NAD+ cofactors. Each subunit consists of a typical NAD-binding domain inserted into a larger core domain that forms the dimer interface. The core domain has a novel chain fold and accommodates the substrate urocanate in a surface depression. The NAD domain sits like a lid on the core domain depression and points with the nicotinamide group to the substrate. Substrate, nicotinamide and five water molecules are completely sequestered in a cavity. Most likely, one of these water molecules hydrates the substrate during catalysis. This cavity has to open for substrate passage, which probably means lifting the NAD domain. The observed atomic arrangement at the active center gives rise to a detailed proposal for the catalytic mechanism that is consistent with published chemical data. As expected, the variability of the residues involved is low, as derived from a family of 58 proteins annotated as urocanases in the data banks. However, one well-embedded member of this family showed a significant deviation at the active center indicating an incorrect annotation.
About this Structure
1UWL is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Structure and action of urocanase., Kessler D, Retey J, Schulz GE, J Mol Biol. 2004 Sep 3;342(1):183-94. PMID:15313616
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