1rpa

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(New page: 200px<br /><applet load="1rpa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpa, resolution 3.0&Aring;" /> '''THREE-DIMENSIONAL STR...)
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'''THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1RPA 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 NAG and TAR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RPA OCA].
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1RPA 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=NAG:'>NAG</scene> and <scene name='pdbligand=TAR:'>TAR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPA OCA].
==Reference==
==Reference==
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[[Category: hydrolase(phosphoric monoester)]]
[[Category: hydrolase(phosphoric monoester)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:46:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:10 2008''

Revision as of 12:53, 21 February 2008


1rpa, resolution 3.0Å

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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 and 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

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