2gpz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2gpz.gif|left|200px]]
{{Seed}}
[[Image:2gpz.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gpz|  PDB=2gpz  |  SCENE=  }}  
{{STRUCTURE_2gpz|  PDB=2gpz  |  SCENE=  }}  


'''Transthyretin-like protein from Salmonella dublin'''
===Transthyretin-like protein from Salmonella dublin===




==Overview==
<!--
The mechanism of binding of thyroid hormones by the transport protein transthyretin (TTR) in vertebrates is structurally well characterised. However, a homologous family of transthyretin-like proteins (TLPs) present in bacteria as well as eukaryotes do not bind thyroid hormones, instead they are postulated to perform a role in the purine degradation pathway and function as 5-hydroxyisourate hydrolases. Here we describe the 2.5 Angstroms X-ray crystal structure of the TLP from the Gram-negative bacterium Salmonella dublin, and compare and contrast its structure with vertebrate TTRs. The overall architecture of the homotetramer is conserved and, despite low sequence homology with vertebrate TTRs, structural differences within the monomer are restricted to flexible loop regions. However, sequence variation at the dimer-dimer interface has profound consequences for the ligand binding site and provides a structural rationalisation for the absence of thyroid hormone binding affinity in bacterial TLPs: the deep, negatively charged thyroxine-binding pocket that characterises vertebrate TTR contrasts with a shallow and elongated, positively charged cleft in S. dublin TLP. We have demonstrated that Sdu_TLP is a 5-hydroxyisourate hydrolase. Furthermore, using site-directed mutagenesis, we have identified three conserved residues located in this cleft that are critical to the enzyme activity. Together our data reveal that the active site of Sdu_TLP corresponds to the thyroxine binding site in TTRs.
The line below this paragraph, {{ABSTRACT_PUBMED_16787778}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16787778 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16787778}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Whisstock, J C.]]
[[Category: Whisstock, J C.]]
[[Category: Salmonella]]
[[Category: Salmonella]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:23:16 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:47:01 2008''

Revision as of 09:47, 27 July 2008

File:2gpz.png

Template:STRUCTURE 2gpz

Transthyretin-like protein from Salmonella dublin

Template:ABSTRACT PUBMED 16787778

About this Structure

2GPZ is a Single protein structure of sequence from Salmonella enterica subsp. enterica serovar dublin. Full crystallographic information is available from OCA.

Reference

The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase., Hennebry SC, Law RH, Richardson SJ, Buckle AM, Whisstock JC, J Mol Biol. 2006 Jun 23;359(5):1389-99. Epub 2006 May 11. PMID:16787778

Page seeded by OCA on Sun Jul 27 12:47:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2gpz&oldid=646684"