1gjv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gjv.jpg|left|200px]]<br /><applet load="1gjv" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1gjv.jpg|left|200px]]
-
caption="1gjv, resolution 2.70&Aring;" />
+
 
-
'''BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE KINASE (BCK) COMPLXED WITH ATP-GAMMA-S'''<br />
+
{{Structure
 +
|PDB= 1gjv |SIZE=350|CAPTION= <scene name='initialview01'>1gjv</scene>, resolution 2.70&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Sap+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=SAP:ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE'>SAP</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.4 Transferred entry: 2.7.11.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.115 2.7.1.115]
 +
|GENE=
 +
}}
 +
 
 +
'''BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE KINASE (BCK) COMPLXED WITH ATP-GAMMA-S'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1GJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=SAP:'>SAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.4 Transferred entry: 2.7.11.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.115 2.7.1.115] Known structural/functional Site: <scene name='pdbsite=AC1:Sap+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJV OCA].
+
1GJV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJV OCA].
==Reference==
==Reference==
-
Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase., Machius M, Chuang JL, Wynn RM, Tomchick DR, Chuang DT, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11218-23. Epub 2001 Sep 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11562470 11562470]
+
Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase., Machius M, Chuang JL, Wynn RM, Tomchick DR, Chuang DT, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11218-23. Epub 2001 Sep 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11562470 11562470]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 27: Line 36:
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:55 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:05 2008''

Revision as of 09:24, 20 March 2008


PDB ID 1gjv

Drag the structure with the mouse to rotate
, resolution 2.70Å
Sites:
Ligands: , , and
Activity: Transferred entry: 2.7.11.4, with EC number 2.7.1.115
Coordinates: save as pdb, mmCIF, xml



BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE KINASE (BCK) COMPLXED WITH ATP-GAMMA-S


Overview

Mitochondrial protein kinases (mPKs) are molecular switches that down-regulate the oxidation of branched-chain alpha-ketoacids and pyruvate. Elevated levels of these metabolites are implicated in disease states such as insulin-resistant Type II diabetes, branched-chain ketoaciduria, and primary lactic acidosis. We report a three-dimensional structure of a member of the mPK family, rat branched-chain alpha-ketoacid dehydrogenase kinase (BCK). BCK features a characteristic nucleotide-binding domain and a four-helix bundle domain. These two domains are reminiscent of modules found in protein histidine kinases (PHKs), which are involved in two-component signal transduction systems. Unlike PHKs, BCK dimerizes through direct interaction of two opposing nucleotide-binding domains. Nucleotide binding to BCK is uniquely mediated by both potassium and magnesium. Binding of ATP induces disorder-order transitions in a loop region at the nucleotide-binding site. These structural changes lead to the formation of a quadruple aromatic stack in the interface between the nucleotide-binding domain and the four-helix bundle domain, where they induce a movement of the top portion of two helices. Phosphotransfer induces further ordering of the loop region, effectively trapping the reaction product ADP, which explains product inhibition in mPKs. The BCK structure is a prototype for all mPKs and will provide a framework for structure-assisted inhibitor design for this family of kinases.

About this Structure

1GJV is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase., Machius M, Chuang JL, Wynn RM, Tomchick DR, Chuang DT, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11218-23. Epub 2001 Sep 18. PMID:11562470

Page seeded by OCA on Thu Mar 20 11:24:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools