1gcu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1gcu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcu, resolution 1.4&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
Line 1: Line 1:
-
[[Image:1gcu.jpg|left|200px]]<br /><applet load="1gcu" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1gcu.jpg|left|200px]]<br /><applet load="1gcu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gcu, resolution 1.4&Aring;" />
caption="1gcu, resolution 1.4&Aring;" />
'''CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A'''<br />
'''CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A'''<br />
 +
 +
==Overview==
 +
Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.
==About this Structure==
==About this Structure==
-
1GCU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Biliverdin_reductase Biliverdin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.24 1.3.1.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GCU OCA].
+
1GCU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Biliverdin_reductase Biliverdin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.24 1.3.1.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCU OCA].
 +
 
 +
==Reference==
 +
Crystal structure of rat biliverdin reductase., Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y, Nat Struct Biol. 2001 Mar;8(3):221-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11224565 11224565]
[[Category: Biliverdin reductase]]
[[Category: Biliverdin reductase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kikuchi, A.]]
[[Category: Kikuchi, A.]]
-
[[Category: Park, S.Y.]]
+
[[Category: Park, S Y.]]
[[Category: Shiro, Y.]]
[[Category: Shiro, Y.]]
[[Category: biliverdin]]
[[Category: biliverdin]]
[[Category: rossmann fold]]
[[Category: rossmann fold]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:57:09 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:49 2008''

Revision as of 10:48, 21 February 2008


1gcu, resolution 1.4Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Overview

Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.

About this Structure

1GCU is a Single protein structure of sequence from Rattus norvegicus. Active as Biliverdin reductase, with EC number 1.3.1.24 Full crystallographic information is available from OCA.

Reference

Crystal structure of rat biliverdin reductase., Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y, Nat Struct Biol. 2001 Mar;8(3):221-5. PMID:11224565

Page seeded by OCA on Thu Feb 21 12:48:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools