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.


1ekf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ekf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ekf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ekf| PDB=1ekf | SCENE= }}
{{STRUCTURE_1ekf| PDB=1ekf | SCENE= }}
-
'''CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)'''
+
===CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)===
-
==Overview==
+
<!--
-
X-ray crystal structures of three forms of human mitochondrial branched-chain aminotransferase (BCAT) were solved by molecular-replacement methods, using Escherichia coli BCAT as the search model. The enzyme is a homodimer and the polypeptide chain of each monomer has two domains. The small domain is composed of residues 1--175 and the large domain is composed of residues 176--365. The active site is close to the dimer interface. The 4'-aldehyde of the PLP cofactor is covalently linked to the epsilon-amino group of the active-site lysine, Lys202, via a Schiff-base linkage in two of the structures. In the third structure, the enzyme is irreversibly inactivated by Tris. The overall fold of the dimer in human mitochondrial BCAT is similar to the structure of two bacterial enzymes, E. coli BCAT and D-amino acid aminotransferase (D-AAT). The residues lining the putative substrate-binding pocket of human BCAT and D-AAT are completely rearranged to allow catalysis with substrates of opposite stereochemistry. In the case of human mitochondrial branched-chain aminotransferase, a hydrogen-bond interaction between the guanidinium group of Arg143 in the first monomer with the side-chain hydroxyl of Tyr70 in the second monomer is important in the formation of the substrate-binding pocket.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11264579}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11264579 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11264579}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Yennawar, N H.]]
[[Category: Yennawar, N H.]]
[[Category: Fold type iv]]
[[Category: Fold type iv]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:12:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:53:33 2008''

Revision as of 21:53, 30 June 2008

Image:1ekf.png

Template:STRUCTURE 1ekf

CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)

Template:ABSTRACT PUBMED 11264579

About this Structure

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

Reference

The structure of human mitochondrial branched-chain aminotransferase., Yennawar N, Dunbar J, Conway M, Hutson S, Farber G, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. PMID:11264579

Page seeded by OCA on Tue Jul 1 00:53:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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