This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1xrf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xrf.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xrf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xrf| PDB=1xrf | SCENE= }}
{{STRUCTURE_1xrf| PDB=1xrf | SCENE= }}
-
'''The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution'''
+
===The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution===
-
==Overview==
+
<!--
-
Dihydroorotases (EC 3.5.2.3) catalyze the reversible cyclization of carbamoyl aspartate to form dihydroorotate in de novo pyrimidine biosynthesis. The X-ray structures of Aquifex aeolicus dihydroorotase in two space groups, C222(1) and C2, were determined at a resolution of 1.7A. These are the first structures of a type I dihydroorotase, a class of molecules that includes the dihydroorotase domain of mammalian CAD. The type I enzymes are more ancient and larger, at 45 kDa, than the type II enzymes exemplified by the 38 kDa Escherichia coli dihydroorotase. Both dihydroorotases are members of the metallo-dependent hydrolase superfamily, whose members have a distorted "TIM barrel" domain containing the active site. However, A.aeolicus dihydroorotase has a second, composite domain, which the E.coli enzyme lacks and has only one of the two zinc atoms present in the E.coli enzyme. A.aeolicus dihydroorotase is unique in exhibiting significant activity only when complexed with aspartate transcarbamoylase, whereas the E.coli dihydroorotase and the CAD dihydroorotase domain are active as free proteins. The latency of A.aeolicus dihydroorotase can be related to two differences between its structure and that of E.coli dihydroorotase: (1) the monoclinic structure has a novel cysteine ligand to the zinc that blocks the active site and possibly functions as a "cysteine switch"; and (2) active site residues that bind the substrate in E.coli dihydroorotase are located in disordered loops in both crystal structures of A.aeolicus dihydroorotase and may function as a disorder-to-order "entropy switch".
+
The line below this paragraph, {{ABSTRACT_PUBMED_15826652}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15826652 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15826652}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Pyrimidine]]
[[Category: Pyrimidine]]
[[Category: Zinc]]
[[Category: Zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:24:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:43:05 2008''

Revision as of 04:43, 28 July 2008

Image:1xrf.png

Template:STRUCTURE 1xrf

The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution

Template:ABSTRACT PUBMED 15826652

About this Structure

1XRF is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

The crystal structure of a novel, latent dihydroorotase from Aquifex aeolicus at 1.7A resolution., Martin PD, Purcarea C, Zhang P, Vaishnav A, Sadecki S, Guy-Evans HI, Evans DR, Edwards BF, J Mol Biol. 2005 May 6;348(3):535-47. PMID:15826652

Page seeded by OCA on Mon Jul 28 07:43:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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