1kt9

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[[Image:1kt9.jpg|left|200px]]<br /><applet load="1kt9" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kt9.jpg|left|200px]]
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caption="1kt9, resolution 1.98&Aring;" />
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'''Crystal Structure of C. elegans Ap4A Hydrolase'''<br />
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{{Structure
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|PDB= 1kt9 |SIZE=350|CAPTION= <scene name='initialview01'>1kt9</scene>, resolution 1.98&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17]
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|GENE= Y37H9A.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])
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}}
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'''Crystal Structure of C. elegans Ap4A Hydrolase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Active as [http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KT9 OCA].
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1KT9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KT9 OCA].
==Reference==
==Reference==
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The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms., Bailey S, Sedelnikova SE, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB, Structure. 2002 Apr;10(4):589-600. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11937063 11937063]
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The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms., Bailey S, Sedelnikova SE, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB, Structure. 2002 Apr;10(4):589-600. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11937063 11937063]
[[Category: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)]]
[[Category: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)]]
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: nudix]]
[[Category: nudix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:50 2008''

Revision as of 10:21, 20 March 2008


PDB ID 1kt9

Drag the structure with the mouse to rotate
, resolution 1.98Å
Gene: Y37H9A.6 (Caenorhabditis elegans)
Activity: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), with EC number 3.6.1.17
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of C. elegans Ap4A Hydrolase


Overview

The crystal structure of C. elegans Ap(4)A hydrolase has been determined for the free enzyme and a binary complex at 2.0 A and 1.8 A, respectively. Ap(4)A hydrolase has a key role in regulating the intracellular Ap(4)A levels and hence potentially the cellular response to metabolic stress and/or differentiation and apoptosis via the Ap(3)A/Ap(4)A ratio. The structures reveal that the enzyme has the mixed alpha/beta fold of the Nudix family and also show how the enzyme binds and locates its substrate with respect to the catalytic machinery of the Nudix motif. These results suggest how the enzyme can catalyze the hydrolysis of a range of related dinucleoside tetraphosphate, but not triphosphate, compounds through precise orientation of key elements of the substrate.

About this Structure

1KT9 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms., Bailey S, Sedelnikova SE, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB, Structure. 2002 Apr;10(4):589-600. PMID:11937063

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