1k75

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k75.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1k75.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k75| PDB=1k75 | SCENE= }}
{{STRUCTURE_1k75| PDB=1k75 | SCENE= }}
-
'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11842181}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11842181 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11842181}}
==About this Structure==
==About this Structure==
Line 42: Line 46:
[[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 Wed Jul 2 09:53:16 2008''

Revision as of 06:53, 2 July 2008

Image:1k75.png

Template:STRUCTURE 1k75

The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.

Template:ABSTRACT PUBMED 11842181

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 Wed Jul 2 09:53:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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