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.


1djl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1djl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1djl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1djl| PDB=1djl | SCENE= }}
{{STRUCTURE_1djl| PDB=1djl | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF HUMAN TRANSHYDROGENASE DOMAIN III WITH BOUND NADP'''
+
===THE CRYSTAL STRUCTURE OF HUMAN TRANSHYDROGENASE DOMAIN III WITH BOUND NADP===
-
==Overview==
+
<!--
-
BACKGROUND: Transhydrogenase, located in the inner membranes of animal mitochondria and the cytoplasmic membranes of bacteria, couples the transfer of reducing equivalents between NAD(H) and NADP(H) to proton pumping. The protein comprises three subunits termed dI, dII and dIII. The dII component spans the membrane. The dI component, which contains the binding site for NAD(+)/NADH, and the dIII component, which has the binding site for NADP(+)/NADPH, protrude from the membrane. Proton pumping is probably coupled to changes in the binding affinities of dIII for NADP(+) and NADPH. RESULTS: The first X-ray structure of the NADP(H)-binding component, dIII, of human heart transhydrogenase is described here at 2.0 A resolution. It comprises a single domain resembling the classical Rossmann fold, but NADP(+) binds to dIII with a reversed orientation. The first betaalphabetaalphabeta motif of dIII contains a Gly-X-Gly-X-X-Ala/Val 'fingerprint', but it has a different function to that in the classical Rossmann structure. The nicotinamide ring of NADP(+) is located on a ridge where it is exposed to interaction with NADH on the dI subunit. Two distinctive features of the dIII structure are helix D/loop D, which projects from the beta sheet, and loop E, which forms a 'lid' over the bound NADP(+). CONCLUSIONS: Helix D/loop D interacts with the bound nucleotide and loop E, and probably interacts with the membrane-spanning dII. Changes in ionisation and conformation in helix D/loop D, resulting from proton translocation through dII, are thought to be responsible for the changes in affinity of dIII for NADP(+) and NADPH that drive the reaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10673423}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10673423 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10673423}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: White, S A.]]
[[Category: White, S A.]]
[[Category: Rossmann fold dinucleotide binding fold reverse binding of nadp]]
[[Category: Rossmann fold dinucleotide binding fold reverse binding of nadp]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:55:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:09:52 2008''

Revision as of 20:09, 30 June 2008

Image:1djl.png

Template:STRUCTURE 1djl

THE CRYSTAL STRUCTURE OF HUMAN TRANSHYDROGENASE DOMAIN III WITH BOUND NADP

Template:ABSTRACT PUBMED 10673423

About this Structure

1DJL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria., White SA, Peake SJ, McSweeney S, Leonard G, Cotton NP, Jackson JB, Structure. 2000 Jan 15;8(1):1-12. PMID:10673423

Page seeded by OCA on Mon Jun 30 23:09:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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