Sandbox Reserved 772: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Jah Ia Yang (talk | contribs) No edit summary |
Jah Ia Yang (talk | contribs) No edit summary |
||
| Line 11: | Line 11: | ||
==Histidinol Dehydrogenase== | ==Histidinol Dehydrogenase== | ||
Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name=" | Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
| Line 18: | Line 18: | ||
==General Information== | ==General Information== | ||
'''Gene Name''': hisD <ref name="info"> | '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
'''Organism''': Escherichia coli (strain K12) <ref name="info"> | '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
'''Classification''': Oxidoreductase | '''Classification''': Oxidoreductase | ||
'''Length''': 434 Amino Acids <ref name="info"> | '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
'''Chains''': A, B <ref name="cite2"> | '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref> | ||
'''Molecular Weight''': | '''Molecular Weight''': | ||
| Line 38: | Line 38: | ||
==Structure== | ==Structure== | ||
HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), 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. The active site, residue His-327, participates in acid-base catalysis <ref name=" | HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), 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. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
48% helical (20 helices; 211 residues) | For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> | ||
16% beta sheet (15 strands; 73 residues) | |||
| Line 51: | Line 50: | ||
[[Image:pathways.jpg]] | [[Image:pathways.jpg]] | ||
This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name=" | This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
==References== | ==References== | ||
<references /> | <references /> | ||
