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.

1gus

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gus.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1gus.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gus| PDB=1gus | SCENE= }}
{{STRUCTURE_1gus| PDB=1gus | SCENE= }}
-
'''MOPII FROM CLOSTRIDIUM PASTEURIANUM (APO1)'''
+
===MOPII FROM CLOSTRIDIUM PASTEURIANUM (APO1)===
-
==Overview==
+
<!--
-
MopII from Clostridium pasteurianum is a molbindin family member. These proteins may serve as intracellular storage facilities for molybdate, which they bind with high specificity. High resolution structures of MopII in a number of states, including the first structure of an apo-molbindin, together with calorimetric data, allow us to describe ligand binding and provide support for the proposed storage function of the protein. MopII assembles as a trimer of dimers and binds eight oxyanions at two types of binding sites located at intersubunit interfaces. Two type 1 sites are on the molecular 3-fold axis and three pairs of type 2 sites occur on the molecular 2-fold axes. The hexamer is largely unaffected by the binding of ligand. Molybdate is admitted to the otherwise inaccessible type 2 binding sites by the movement of the N-terminal residues of each protein chain. This contrasts with the structurally related molybdate-dependent transcriptional regulator ModE, which undergoes extensive conformational rearrangements on ligand binding. Despite similarities between the binding sites of ModE and the type 2 sites of MopII the molbindin has a significantly reduced ligand affinity, due, in part, to the high density of negative charges at the center of the hexamer. In the absence of ligand this effects the movement of an important lysine side chain, thereby partially inactivating the binding sites. The differences are consistent with a biological role in molybdate storage/buffering.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11836258}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11836258 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11836258}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Molybdate binding]]
[[Category: Molybdate binding]]
[[Category: Mop]]
[[Category: Mop]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:02:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:07:00 2008''

Revision as of 03:07, 1 July 2008

Image:1gus.png

Template:STRUCTURE 1gus

MOPII FROM CLOSTRIDIUM PASTEURIANUM (APO1)

Template:ABSTRACT PUBMED 11836258

About this Structure

1GUS is a Single protein structure of sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA.

Reference

Passive acquisition of ligand by the MopII molbindin from Clostridium pasteurianum: structures of apo and oxyanion-bound forms., Schuttelkopf AW, Harrison JA, Boxer DH, Hunter WN, J Biol Chem. 2002 Apr 26;277(17):15013-20. Epub 2002 Feb 8. PMID:11836258

Page seeded by OCA on Tue Jul 1 06:07:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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