Sandbox Reserved 328: Difference between revisions
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Structural | Structural | ||
==Overall Structure== | ==Overall Structure== | ||
HisD is a homodimer, with each subunit consisting of a globule segment, and an extending tail. The two larger domains (1 and 2) are within the globule, and domains 3 and 4 are found in the tail. | HisD is a homodimer, with each subunit consisting of a globule segment, and an extending tail. The two larger domains (1 and 2) are within the globule, and domains 3 and 4 are found in the tail. The cores of both domains (residues 124–236 in domain 1 & 237–381 in domain 2) adopt incomplete Rossmann folds, which lack the last strand-helix hairpin<ref name="1kar" />. To carry out its function, HisD relies on the presence of one Zn2+ cation per monomer, not for catalysis, but for substrate binding. | ||
<scene name='Sandbox_Reserved_328/Beta_sheets/1'>Beta Sheets</scene> | <scene name='Sandbox_Reserved_328/Beta_sheets/1'>Beta Sheets</scene> | ||
Revision as of 05:38, 3 April 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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| 1kar, resolution 2.10Å (default scene) | |||||||||||||
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| Ligands: | HSM, ZN | ||||||||||||
| Non-Standard Residues: | MSE | ||||||||||||
| Gene: | HISD (Escherichia coli) | ||||||||||||
| Activity: | Histidinol dehydrogenase, with EC number 1.1.1.23 | ||||||||||||
| Related: | 1k75, 1kae, 1kah | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
L-Histidinol Dehydrogenase
The enzyme l-histidinol dehydrogenase (HisD)
ALL INFORMATION IN HERE!!! sub-headings for topics of interest (mechanism, binding sites, etc.) Basic information, current knowledge of areas found, etc. Structural
Overall Structure
HisD is a homodimer, with each subunit consisting of a globule segment, and an extending tail. The two larger domains (1 and 2) are within the globule, and domains 3 and 4 are found in the tail. The cores of both domains (residues 124–236 in domain 1 & 237–381 in domain 2) adopt incomplete Rossmann folds, which lack the last strand-helix hairpin[1]. To carry out its function, HisD relies on the presence of one Zn2+ cation per monomer, not for catalysis, but for substrate binding.
Enzymatic mechanism
Other information??
References
- ↑ 1.0 1.1 1.2 Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:11842181 doi:10.1073/pnas.022476199
