We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1w1u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w1u.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1w1u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w1u| PDB=1w1u | SCENE= }}
{{STRUCTURE_1w1u| PDB=1w1u | SCENE= }}
-
'''INACTIVE UROCANASE-SA COCRYSTALLIZED WITH UROCANATE'''
+
===INACTIVE UROCANASE-SA COCRYSTALLIZED WITH UROCANATE===
-
==Overview==
+
<!--
-
Urocanase (EC 4.2.1.49) from Pseudomonas putida was crystallized after removing one of the seven free thiol groups. The crystal structure was solved by multiwavelength anomalous diffraction (MAD) using a seleno-methionine derivative and then refined at 1.14 A resolution. The enzyme is a symmetric homodimer of 2 x 557 amino acid residues with tightly bound NAD+ cofactors. Each subunit consists of a typical NAD-binding domain inserted into a larger core domain that forms the dimer interface. The core domain has a novel chain fold and accommodates the substrate urocanate in a surface depression. The NAD domain sits like a lid on the core domain depression and points with the nicotinamide group to the substrate. Substrate, nicotinamide and five water molecules are completely sequestered in a cavity. Most likely, one of these water molecules hydrates the substrate during catalysis. This cavity has to open for substrate passage, which probably means lifting the NAD domain. The observed atomic arrangement at the active center gives rise to a detailed proposal for the catalytic mechanism that is consistent with published chemical data. As expected, the variability of the residues involved is low, as derived from a family of 58 proteins annotated as urocanases in the data banks. However, one well-embedded member of this family showed a significant deviation at the active center indicating an incorrect annotation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15313616}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15313616 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15313616}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Urocanase]]
[[Category: Urocanase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:02:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:50:59 2008''

Revision as of 18:51, 28 July 2008

Image:1w1u.png

Template:STRUCTURE 1w1u

INACTIVE UROCANASE-SA COCRYSTALLIZED WITH UROCANATE

Template:ABSTRACT PUBMED 15313616

About this Structure

1W1U is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Structure and action of urocanase., Kessler D, Retey J, Schulz GE, J Mol Biol. 2004 Sep 3;342(1):183-94. PMID:15313616

Page seeded by OCA on Mon Jul 28 21:50:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w1u"
Personal tools