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.

3pga

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3pga.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3pga.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3pga| PDB=3pga | SCENE= }}
{{STRUCTURE_3pga| PDB=3pga | SCENE= }}
-
'''STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE'''
+
===STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE===
-
==Overview==
+
<!--
-
The amino acid sequence and a 2-A-resolution crystallographic structure of Pseudomonas 7A glutaminase-asparaginase (PGA) have been determined. PGA, which belongs to the family of tetrameric bacterial amidohydrolases, deamidates glutamine and asparagine. The amino acid sequence of PGA has a high degree of similarity to the sequences of other members of the family. PGA has the same fold as other bacterial amidohydrolases, with the exception of the position of a 20-residue loop that forms part of the active site. In the PGA structure presented here, the active site loop is observed clearly in only one monomer, in an open position, with a conformation different from that observed for other amidohydrolases. In the other three monomers the loop is disordered and cannot be traced. This phenomenon is probably a direct consequence of a very low occupancy of product(s) of the enzymatic reaction bound in the active sites of PGA in these crystals. The active sites are composed of a rigid part and the flexible loop. The rigid part consists of the residues directly involved in the catalytic reaction as well as residues that assist in orienting the substrate. Two residues that are important for activity residue on the flexible loop. We suggest that the flexible loops actively participate in the transport of substrate and product molecules through the amidohydrolase active sites and participate in orienting the substrate molecules properly in relation to the catalytic residues.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8068664}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8068664 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8068664}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: Bacterial amidohydrolase]]
[[Category: Bacterial amidohydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:10:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:01:32 2008''

Revision as of 10:01, 3 July 2008

Image:3pga.png

Template:STRUCTURE 3pga

STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE

Template:ABSTRACT PUBMED 8068664

About this Structure

3PGA is a Single protein structure of sequence from Pseudomonas sp. 7a. Full crystallographic information is available from OCA.

Reference

Structural characterization of Pseudomonas 7A glutaminase-asparaginase., Lubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL, Biochemistry. 1994 Aug 30;33(34):10257-65. PMID:8068664

Page seeded by OCA on Thu Jul 3 13:01:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3pga"
Personal tools