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.

2g2n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2g2n.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2g2n.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2g2n| PDB=2g2n | SCENE= }}
{{STRUCTURE_2g2n| PDB=2g2n | SCENE= }}
-
'''Crystal Structure of E.coli transthyretin-related protein with bound Zn'''
+
===Crystal Structure of E.coli transthyretin-related protein with bound Zn===
-
==Overview==
+
<!--
-
The transthyretin-related protein (TRP) family comprises proteins predicted to be structurally related to the homotetrameric transport protein transthyretin (TTR). The function of TRPs is not yet fully established, but recent data suggest that they are involved in purine catabolism. We have determined the three-dimensional structure of the Escherichia coli TRP in two crystal forms; one at 1.65 A resolution in the presence of zinc, and the other at 2.1 A resolution in the presence of zinc and bromide. The structures revealed five zinc-ion-binding sites per monomer. Of these, the zinc ions bound at sites I and II are coordinated in tetrahedral geometries to the side chains of residues His9, His96, His98, Ser114, and three water molecules at the putative ligand-binding site. Of these four residues, His9, His98, and Ser114 are conserved. His9 and His98 bind the central zinc (site I) together with two water molecules. The side chain of His98 also binds to the zinc ion at site II. Bromide ions bind at site I only, replacing one of the water molecules coordinated to the zinc ion. The C-terminal four amino acid sequence motif Y-[RK]-G-[ST] constitutes the signature sequence of the TRP family. Two Tyr111 residues form direct hydrogen bonds to each other over the tetramer interface at the area, which in TTR constitutes the rear part of its thyroxine-binding channel. The putative substrate/ligand-binding channel of TRP is consequently shallower and broader than its counterpart in TTR.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16723258}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16723258 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16723258}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Transthyretin]]
[[Category: Transthyretin]]
[[Category: Transthyretin-related protein]]
[[Category: Transthyretin-related protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:37:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:32:26 2008''

Revision as of 08:32, 28 July 2008

Image:2g2n.png

Template:STRUCTURE 2g2n

Crystal Structure of E.coli transthyretin-related protein with bound Zn

Template:ABSTRACT PUBMED 16723258

About this Structure

2G2N is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The transthyretin-related protein: structural investigation of a novel protein family., Lundberg E, Backstrom S, Sauer UH, Sauer-Eriksson AE, J Struct Biol. 2006 Sep;155(3):445-57. Epub 2006 May 8. PMID:16723258

Page seeded by OCA on Mon Jul 28 11:32:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2g2n"
Personal tools