1mh9

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(New page: 200px<br /> <applet load="1mh9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mh9, resolution 1.80&Aring;" /> '''Crystal Structure A...)
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<applet load="1mh9" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure Analysis of deoxyribonucleotidase'''<br />
'''Crystal Structure Analysis of deoxyribonucleotidase'''<br />
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==About this Structure==
==About this Structure==
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1MH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MH9 OCA].
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1MH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MH9 OCA].
==Reference==
==Reference==
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[[Category: rossman fold]]
[[Category: rossman fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:24:16 2008''

Revision as of 14:24, 15 February 2008


1mh9, resolution 1.80Å

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Crystal Structure Analysis of deoxyribonucleotidase

Overview

5' nucleotidases are ubiquitous enzymes that dephosphorylate nucleoside, monophosphates and participate in the regulation of nucleotide pools. The, mitochondrial 5'-(3') deoxyribonucleotidase (dNT-2) specifically, dephosphorylates dUMP and dTMP, thereby protecting mitochondrial DNA, replication from excess dTTP. We have solved the structure of dNT-2, the, first of a mammalian 5' nucleotidase. The structure reveals a relationship, to the HAD family, members of which use an aspartyl nucleophile as their, common catalytic strategy, with a phosphoserine phosphatase as the most, similar neighbor. A structure-based sequence alignment of dNT-2 with other, 5' nucleotidases also suggests a common origin for these enzymes. Here we, study the structures of dNT-2 in complex with bound phosphate and, beryllium trifluoride plus thymidine as model for a phosphoenzyme-product, complex. Based on these structures, determinants for substrate specificity, recognition and the catalytic action of dNT-2 are outlined.

About this Structure

1MH9 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as 5'-nucleotidase, with EC number 3.1.3.5 Full crystallographic information is available from OCA.

Reference

Crystal structure of a human mitochondrial deoxyribonucleotidase., Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P, Nat Struct Biol. 2002 Oct;9(10):779-87. PMID:12352955

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