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.


1bi1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bi1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1bi1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bi1| PDB=1bi1 | SCENE= }}
{{STRUCTURE_1bi1| PDB=1bi1 | SCENE= }}
-
'''STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR'''
+
===STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR===
-
==Overview==
+
<!--
-
The diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae is a divalent metal-activated repressor of chromosomal genes that encode proteins responsible for siderophore-mediated iron uptake and also of the gene of certain corynebacteriophages that encodes diphtheria toxin. DtxR consists of two 25.3-kDa three-domain subunits and is a member of a family of related repressor proteins in several Gram-positive bacterial species, some of which are important human pathogens. In this paper, we report on the first high resolution crystal structures of apo-DtxR in two related space groups. In addition, crystal structures of Zn-DtxR were determined in the same two space groups. The resolutions of the structures range from 2.2 to 2.4 A. The four refined models of the apo- and the holo-repressor exhibit quite similar metal binding centers, which do, however, show higher thermal motion in the apo-structures. All four structures reported differ from each other in one important aspect. The N-terminal DNA-binding domain and the last 20 residues of the dimerization domain of each subunit move significantly with respect to the core of the DtxR dimer, which consists of residues 74-120 from both subunits. These results provide the first indication of a conformational change that may occur upon binding of the holo-repressor to DNA.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9712865}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9712865 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9712865}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Repressor]]
[[Category: Repressor]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:32:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:11:51 2008''

Revision as of 16:11, 30 June 2008

Image:1bi1.png

Template:STRUCTURE 1bi1

STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR

Template:ABSTRACT PUBMED 9712865

About this Structure

1BI1 is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.

Reference

Motion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor (DtxR) revealed in the crystal structures of apo- and holo-DtxR., Pohl E, Holmes RK, Hol WG, J Biol Chem. 1998 Aug 28;273(35):22420-7. PMID:9712865

Page seeded by OCA on Mon Jun 30 19:11:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bi1"
Personal tools