1rpa
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1rpa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpa, resolution 3.0Å" /> '''THREE-DIMENSIONAL STR...)
Next diff →
Revision as of 23:38, 20 November 2007
|
THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE
Overview
The crystal structure of recombinant rat prostatic acid phosphatase in, complex with the inhibitor L(+)-tartrate was determined to 3-A resolution, with protein crystallographic methods. The inhibitor binds at the carboxyl, end of the parallel strands of the alpha/beta domain. One of the carboxyl, groups of the tartrate molecule interacts with the conserved residues, Arg-11, His-12, and Arg-15, which form part of the phosphate binding site., Furthermore, the C2 and C3 hydroxyl groups interact with His-257 and, Arg-79. The second carboxyl group is close to Arg-79 but makes no direct, hydrogen bonds to the protein. A sequence comparison between, tartrate-sensitive and -resistant acid phosphatases suggests that these, enzymes have different three-dimensional structures.
About this Structure
1RPA is a Single protein structure of sequence from Rattus norvegicus with NAG and TAR as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate., Lindqvist Y, Schneider G, Vihko P, J Biol Chem. 1993 Oct 5;268(28):20744-6. PMID:8407898
Page seeded by OCA on Wed Nov 21 01:46:09 2007
