This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1stz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1stz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1stz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1stz| PDB=1stz | SCENE= }}
{{STRUCTURE_1stz| PDB=1stz | SCENE= }}
-
'''Crystal structure of a hypothetical protein at 2.2 A resolution'''
+
===Crystal structure of a hypothetical protein at 2.2 A resolution===
-
==Overview==
+
<!--
-
All cells have a defense mechanism against a sudden heat-shock stress. Commonly, they express a set of proteins that protect cellular proteins from being denatured by heat. Among them, GroE and DnaK chaperones are representative defending systems, and their transcription is regulated by a heat-shock repressor protein HrcA. HrcA repressor controls the transcription of groE and dnaK operons by binding the palindromic CIRCE element, presumably as a dimer, and the activity of HrcA repressor is modulated by GroE chaperones. Here, we report the first crystal structure of a heat-inducible transcriptional repressor, HrcA, from Thermotoga maritima at 2.2A resolution. The Tm_HrcA protein crystallizes as a dimer. The monomer is composed of three domains: an N-terminal winged helix-turn-helix domain (WH), a GAF-like domain, and an inserted dimerizing domain (IDD). The IDD shows a unique structural fold with an anti-parallel beta-sheet composed of three beta-strands sided by four alpha-helices. The Tm_HrcA dimer structure is formed through hydrophobic contact between the IDDs and a limited contact that involves conserved residues between the GAF-like domains. In the overall dimer structure, the two WH domains are exposed, but the conformation of these two domains seems to be incompatible with DNA binding. We suggest that our structure may represent an inactive form of the HrcA repressor. Structural implication on how the inactive form of HrcA may be converted to the active form by GroEL binding to a conserved C-terminal sequence region of HrcA is discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15979091}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15979091 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15979091}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Psi]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:07:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:35:53 2008''

Revision as of 07:35, 28 July 2008

Image:1stz.png

Template:STRUCTURE 1stz

Crystal structure of a hypothetical protein at 2.2 A resolution

Template:ABSTRACT PUBMED 15979091

About this Structure

1STZ is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Crystal structure of a heat-inducible transcriptional repressor HrcA from Thermotoga maritima: structural insight into DNA binding and dimerization., Liu J, Huang C, Shin DH, Yokota H, Jancarik J, Kim JS, Adams PD, Kim R, Kim SH, J Mol Biol. 2005 Jul 29;350(5):987-96. PMID:15979091

Page seeded by OCA on Mon Jul 28 10:35:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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