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2mas

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(New page: 200px<br /> <applet load="2mas" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mas, resolution 2.3&Aring;" /> '''PURINE NUCLEOSIDE HY...)
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==About this Structure==
==About this Structure==
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2MAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]] with CA and PIR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.1 3.2.2.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MAS OCA]].
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2MAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]] with CA and PIR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Purine_nucleosidase Purine nucleosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.1 3.2.2.1]]. Structure known Active Sites: S1, S2, S3 and S4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MAS OCA]].
==Reference==
==Reference==
Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor., Degano M, Almo SC, Sacchettini JC, Schramm VL, Biochemistry. 1998 May 5;37(18):6277-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9572842 9572842]
Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor., Degano M, Almo SC, Sacchettini JC, Schramm VL, Biochemistry. 1998 May 5;37(18):6277-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9572842 9572842]
[[Category: Crithidia fasciculata]]
[[Category: Crithidia fasciculata]]
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[[Category: Purine nucleosidase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Degano, M.]]
[[Category: Degano, M.]]
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[[Category: uridine]]
[[Category: uridine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:52:47 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:09:12 2007''

Revision as of 10:04, 30 October 2007


2mas, resolution 2.3Å

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PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

Overview

Nucleoside N-ribohydrolases are targets for disruption of purine salvage, in the protozoan parasites. The structure of a trypanosomal, N-ribohydrolase in complex with a transition-state inhibitor is reported, at 2.3 A resolution. The nonspecific nucleoside hydrolase from Crithidia, fasciculata cocrystallized with p-aminophenyliminoribitol reveals tightly, bound Ca2+ as a catalytic site ligand. The complex with the, transition-state inhibitor is characterized by (1) large protein, conformational changes to create a hydrophobic leaving group site (2), C3'-exo geometry for the inhibitor, typical of a ribooxocarbenium ion (3), stabilization of the ribooxocarbenium analogue between the neighboring, group 5'-hydroxyl and bidentate hydrogen bonds to Asn168; and (4), octacoordinate Ca2+ orients a ... [(full description)]

About this Structure

2MAS is a [Single protein] structure of sequence from [Crithidia fasciculata] with CA and PIR as [ligands]. Active as [Purine nucleosidase], with EC number [3.2.2.1]. Structure known Active Sites: S1, S2, S3 and S4. Full crystallographic information is available from [OCA].

Reference

Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor., Degano M, Almo SC, Sacchettini JC, Schramm VL, Biochemistry. 1998 May 5;37(18):6277-85. PMID:9572842

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