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.

To get started:

Click the edit this page tab at the top. Save the page after each step, then edit it again.
Click the 3D button (when editing, above the wikitext box) to insert Jmol.
show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

1kar, resolution 2.10Å ()

Ligands:

,

Non-Standard Residues:

Gene:

HISD (Escherichia coli)

Activity:

Histidinol dehydrogenase, with EC number 1.1.1.23

Related:

1k75, 1kae, 1kah

Structural annotation:
Resources:	CATH : 1Kara02, 1Kara01, 1Karb01, 1Karb02 InterPro : Ipr012131, Ipr001692 Pfam : PF00815 SCOP : d1kara_, d1karb_ UniProt : P06988

Functional annotation:
Biological process:	histidine biosynthetic process amino acid biosynthetic process
Molecular function:	metal ion binding NAD binding histidinol dehydrogenase activity oxidoreductase activity zinc ion binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

L-Histidinol DehydrogenaseL-Histidinol Dehydrogenase

The enzyme l-histidinol dehydrogenase (HisD) Basic information, current knowledge of areas found, etc. Structural

Overall StructureOverall 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. The Zn2+ cation is located at the bottom of the cavity occupied by the substrate and is octahedrally coordinated by four seperate residues. Along with Zn, the coordination of the substrate in the active site is assisted by the large degree of secondary structure present in the protein. The substrate binds in a deep pocket formed at the dimer interface between domains 1, 2, and 4, with most interactions being with residues at the N-terminal end of the β-sheet found within domain 2. Large amounts of secondary structure both in the form of and are present, and serve to provide a base for the overall structure of the molecule.

Enzymatic mechanismEnzymatic mechanism

Other informationOther information

^[1]. ^[1].

ReferencesReferences

↑ ^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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Simon Loewen

[1kar-1] 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

[1]

Sandbox Reserved 328

Contents