1k75

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1k75.jpg|left|200px]]
[[Image:1k75.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1k75 |SIZE=350|CAPTION= <scene name='initialview01'>1k75</scene>, resolution 1.75&Aring;
+
The line below this paragraph, containing "STRUCTURE_1k75", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|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>
+
or leave the SCENE parameter empty for the default display.
-
|GENE= hisD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1k75| PDB=1k75 | SCENE= }}
-
|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>
+
-
}}
+
'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.'''
'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.'''
Line 35: Line 32:
[[Category: Sivaraman, J.]]
[[Category: Sivaraman, J.]]
[[Category: 4 domain]]
[[Category: 4 domain]]
-
[[Category: bsgi]]
+
[[Category: Bsgi]]
-
[[Category: hisd]]
+
[[Category: Hisd]]
-
[[Category: homodimer]]
+
[[Category: Homodimer]]
-
[[Category: l-histidine biosynthesis]]
+
[[Category: L-histidine biosynthesis]]
-
[[Category: l-histidinol dehydrogenase]]
+
[[Category: L-histidinol dehydrogenase]]
-
[[Category: montreal-kingston bacterial structural genomics initiative]]
+
[[Category: Montreal-kingston bacterial structural genomics initiative]]
-
[[Category: nad cofactor]]
+
[[Category: Nad cofactor]]
-
[[Category: rossman fold]]
+
[[Category: Rossman fold]]
-
[[Category: structural genomic]]
+
[[Category: Structural genomic]]
-
[[Category: zinc]]
+
[[Category: Zinc]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:23:20 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:20 2008''
+

Revision as of 19:23, 2 May 2008

Image:1k75.jpg

Template:STRUCTURE 1k75

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 Fri May 2 22:23:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k75"
Personal tools