1nvi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nvi.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1nvi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nvi| PDB=1nvi | SCENE= }}
{{STRUCTURE_1nvi| PDB=1nvi | SCENE= }}
-
'''Orthorhombic Crystal Form of Molybdopterin Synthase'''
+
===Orthorhombic Crystal Form of Molybdopterin Synthase===
-
==Overview==
+
<!--
-
Molybdenum cofactor biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in cofactor biosynthesis in humans lead to a severe and usually fatal disease. The molybdenum cofactor contains a tricyclic pyranopterin, termed molybdopterin, that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE) and small (MoaD) subunit. The crystal structure of molybdopterin synthase revealed a heterotetrameric enzyme in which the C terminus of each MoaD subunit is deeply inserted into a MoaE subunit to form the active site. In the activated form of the enzyme, the MoaD C terminus is present as a thiocarboxylate. The present study identified the position of the thiocarboxylate sulfur by exploiting the anomalous signal originating from the sulfur atom. The structure of molybdopterin synthase in a novel crystal form revealed a binding pocket for the terminal phosphate of molybdopterin, the product of the enzyme, and suggested a binding site for the pterin moiety present in precursor Z and molybdopterin. Finally, the crystal structure of the MoaE homodimer provides insights into the conformational changes accompanying binding of the MoaD subunit.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12571227}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12571227 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12571227}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Molybdenum cofactor biosynthesis]]
[[Category: Molybdenum cofactor biosynthesis]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:01:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:59:14 2008''

Revision as of 03:59, 29 July 2008

Image:1nvi.png

Template:STRUCTURE 1nvi

Orthorhombic Crystal Form of Molybdopterin Synthase

Template:ABSTRACT PUBMED 12571227

About this Structure

1NVI is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural studies of molybdopterin synthase provide insights into its catalytic mechanism., Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H, J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. PMID:12571227

Page seeded by OCA on Tue Jul 29 06:59:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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