1het

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1het" [edit=sysop:move=sysop])
Line 1: Line 1:
[[Image:1het.png|left|200px]]
[[Image:1het.png|left|200px]]
-
<!--
 
-
The line below this paragraph, containing "STRUCTURE_1het", creates the "Structure Box" on the page.
 
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 
-
or leave the SCENE parameter empty for the default display.
 
-
-->
 
{{STRUCTURE_1het| PDB=1het | SCENE= }}
{{STRUCTURE_1het| PDB=1het | SCENE= }}
===ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH===
===ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH===
- 
-
<!--
 
-
The line below this paragraph, {{ABSTRACT_PUBMED_11134046}}, adds the Publication Abstract to the page
 
-
(as it appears on PubMed at http://www.pubmed.gov), where 11134046 is the PubMed ID number.
 
-
-->
 
{{ABSTRACT_PUBMED_11134046}}
{{ABSTRACT_PUBMED_11134046}}
==About this Structure==
==About this Structure==
-
[[1het]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HET OCA].
+
[[1het]] is a 2 chain structure of [[Alcohol dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HET OCA].
 +
 
 +
==See Also==
 +
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
==Reference==
==Reference==
-
<ref group="xtra">PMID:11134046</ref><ref group="xtra">PMID:10529241</ref><ref group="xtra">PMID:9220961</ref><ref group="xtra">PMID:15299812</ref><ref group="xtra">PMID:15299346</ref><ref group="xtra">PMID:3771574</ref><ref group="xtra">PMID:6098306</ref><ref group="xtra">PMID:6351056</ref><ref group="xtra">PMID:6362718</ref><ref group="xtra">PMID:6753930</ref><ref group="xtra">PMID:178875</ref><ref group="xtra">PMID:4365379</ref><references group="xtra"/>
+
<ref group="xtra">PMID:011134046</ref><ref group="xtra">PMID:010529241</ref><ref group="xtra">PMID:009220961</ref><ref group="xtra">PMID:015299812</ref><ref group="xtra">PMID:015299346</ref><ref group="xtra">PMID:003771574</ref><ref group="xtra">PMID:006098306</ref><ref group="xtra">PMID:006351056</ref><ref group="xtra">PMID:006362718</ref><ref group="xtra">PMID:006753930</ref><ref group="xtra">PMID:000178875</ref><ref group="xtra">PMID:004365379</ref><references group="xtra"/>
[[Category: Alcohol dehydrogenase]]
[[Category: Alcohol dehydrogenase]]
[[Category: Equus caballus]]
[[Category: Equus caballus]]

Revision as of 17:48, 26 July 2012

Template:STRUCTURE 1het

Contents

ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH

Template:ABSTRACT PUBMED 11134046

About this Structure

1het is a 2 chain structure of Alcohol dehydrogenase with sequence from Equus caballus. Full crystallographic information is available from OCA.

See Also

Reference

  • Meijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES. On the enzymatic activation of NADH. J Biol Chem. 2001 Mar 23;276(12):9316-21. Epub 2000 Dec 28. PMID:11134046 doi:10.1074/jbc.M010870200
  • Ramaswamy S, Park DH, Plapp BV. Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer. Biochemistry. 1999 Oct 19;38(42):13951-9. PMID:10529241
  • Adolph HW, Kiefer M, Cedergren-Zeppezauer E. Electrostatic effects in the kinetics of coenzyme binding to isozymes of alcohol dehydrogenase from horse liver. Biochemistry. 1997 Jul 22;36(29):8743-54. PMID:9220961 doi:10.1021/bi970398k
  • Al-Karadaghi S, Cedergren-Zeppezauer ES, Dauter Z, Wilson KS. Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):805-13. PMID:15299812 doi:10.1107/S090744499500045X
  • Al-Karadaghi S, Cedergren-Zeppezauer ES, Hovmoller S. Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):793-807. PMID:15299346 doi:http://dx.doi.org/10.1107/S0907444994005263
  • Colonna-Cesari F, Perahia D, Karplus M, Eklund H, Braden CI, Tapia O. Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode. J Biol Chem. 1986 Nov 15;261(32):15273-80. PMID:3771574
  • Eklund H, Samama JP, Jones TA. Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Biochemistry. 1984 Dec 4;23(25):5982-96. PMID:6098306
  • Schneider G, Eklund H, Cedergren-Zeppezauer E, Zeppezauer M. Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives. Proc Natl Acad Sci U S A. 1983 Sep;80(17):5289-93. PMID:6351056
  • Cedergren-Zeppezauer E. Crystal-structure determination of reduced nicotinamide adenine dinucleotide complex with horse liver alcohol dehydrogenase maintained in its apo conformation by zinc-bound imidazole. Biochemistry. 1983 Dec 6;22(25):5761-72. PMID:6362718
  • Cedergren-Zeppezauer E, Samama JP, Eklund H. Crystal structure determinations of coenzyme analogue and substrate complexes of liver alcohol dehydrogenase: binding of 1,4,5,6-tetrahydronicotinamide adenine dinucleotide and trans-4-(N,N-dimethylamino)cinnamaldehyde to the enzyme. Biochemistry. 1982 Sep 28;21(20):4895-908. PMID:6753930
  • Eklund H, Nordstrom B, Zeppezauer E, Soderlund G, Ohlsson I, Boiwe T, Soderberg BO, Tapia O, Branden CI, Akeson A. Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. J Mol Biol. 1976 Mar 25;102(1):27-59. PMID:178875
  • Branden CI, Eklund H, Nordstrom B, Boiwe T, Soderlund G, Zeppezauer E, Ohlsson I, Akeson A. Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2439-42. PMID:4365379

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools