1k75: Difference between revisions
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'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.''' | {{Structure | ||
|PDB= 1k75 |SIZE=350|CAPTION= <scene name='initialview01'>1k75</scene>, resolution 1.75Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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] | |||
|GENE= hisD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1K75 is a [ | 1K75 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11842181 11842181] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Histidinol dehydrogenase]] | [[Category: Histidinol dehydrogenase]] | ||
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[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: 4 | [[Category: 4 domain]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
[[Category: hisd]] | [[Category: hisd]] | ||
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[[Category: nad cofactor]] | [[Category: nad cofactor]] | ||
[[Category: rossman fold]] | [[Category: rossman fold]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:13:28 2008'' | ||
Revision as of 13:13, 20 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | hisD (Escherichia coli) | ||||||
| Activity: | Histidinol dehydrogenase, with EC number 1.1.1.23 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
OverviewOverview
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 StructureAbout this Structure
1K75 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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.
- GOL
- SO4
- 4 domain
- Bsgi
- Hisd
- Homodimer
- L-histidine biosynthesis
- L-histidinol dehydrogenase
- Montreal-kingston bacterial structural genomics initiative
- Nad cofactor
- Rossman fold
- Structural genomic
- Zinc