1k75
From Proteopedia
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|PDB= 1k75 |SIZE=350|CAPTION= <scene name='initialview01'>1k75</scene>, resolution 1.75Å | |PDB= 1k75 |SIZE=350|CAPTION= <scene name='initialview01'>1k75</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Histidinol_dehydrogenase Histidinol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.23 1.1.1.23] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol_dehydrogenase Histidinol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.23 1.1.1.23] </span> |
|GENE= hisD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= hisD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k75 OCA], [http://www.ebi.ac.uk/pdbsum/1k75 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k75 RCSB]</span> | ||
}} | }} | ||
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[[Category: Schrag, J.]] | [[Category: Schrag, J.]] | ||
[[Category: Sivaraman, J.]] | [[Category: Sivaraman, J.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: 4 domain]] | [[Category: 4 domain]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:20 2008'' |
Revision as of 18:44, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | hisD (Escherichia coli) | ||||||
| Activity: | Histidinol dehydrogenase, with EC number 1.1.1.23 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
Overview
The histidine biosynthetic pathway is an ancient one found in bacteria, archaebacteria, fungi, and plants that converts 5-phosphoribosyl 1-pyrophosphate to l-histidine in 10 enzymatic reactions. This pathway provided a paradigm for the operon, transcriptional regulation of gene expression, and feedback inhibition of a pathway. l-histidinol dehydrogenase (HisD, EC ) catalyzes the last two steps in the biosynthesis of l-histidine: sequential NAD-dependent oxidations of l-histidinol to l-histidinaldehyde and then to l-histidine. HisD functions as a homodimer and requires the presence of one Zn(2+) cation per monomer. We have determined the three-dimensional structure of Escherichia coli HisD in the apo state as well as complexes with substrate, Zn(2+), and NAD(+) (best resolution is 1.7 A). Each monomer is made of four domains, whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. Zn(2+) plays a crucial role in substrate binding but is not directly involved in catalysis. The active site residue His-327 participates in acid-base catalysis, whereas Glu-326 activates a water molecule. NAD(+) binds weakly to one of the Rossmann fold domains in a manner different from that previously observed for other proteins having a Rossmann fold.
About this Structure
1K75 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase., Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M, Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:11842181
Page seeded by OCA on Sun Mar 30 21:44:20 2008
Categories: Escherichia coli | Histidinol dehydrogenase | Single protein | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Barbosa, J A.R G. | Cygler, M. | Larocque, R. | Li, Y. | Matte, A. | Schrag, J. | Sivaraman, J. | 4 domain | Bsgi | Hisd | Homodimer | L-histidine biosynthesis | L-histidinol dehydrogenase | Montreal-kingston bacterial structural genomics initiative | Nad cofactor | Rossman fold | Structural genomic | Zinc
