2oip
From Proteopedia
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[[Image:2oip.png|left|200px]] | [[Image:2oip.png|left|200px]] | ||
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{{STRUCTURE_2oip| PDB=2oip | SCENE= }} | {{STRUCTURE_2oip| PDB=2oip | SCENE= }} | ||
===Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis=== | ===Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis=== | ||
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{{ABSTRACT_PUBMED_17580969}} | {{ABSTRACT_PUBMED_17580969}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2oip]] is a 5 chain structure of [[Dihydrofolate reductase]] with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIP OCA]. | + | [[2oip]] is a 5 chain structure of [[Dihydrofolate reductase]] and [[Thymidylate synthase]] with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIP OCA]. |
==See Also== | ==See Also== | ||
| - | *[[Dihydrofolate reductase]] | + | *[[Dihydrofolate reductase|Dihydrofolate reductase]] |
| + | *[[Thymidylate synthase|Thymidylate synthase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:017580969</ref><ref group="xtra">PMID:018672899</ref><references group="xtra"/> |
[[Category: Cryptosporidium hominis]] | [[Category: Cryptosporidium hominis]] | ||
[[Category: Martucci, W E.]] | [[Category: Martucci, W E.]] | ||
Revision as of 06:56, 27 July 2012
Contents |
Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis
Template:ABSTRACT PUBMED 17580969
About this Structure
2oip is a 5 chain structure of Dihydrofolate reductase and Thymidylate synthase with sequence from Cryptosporidium hominis. Full crystallographic information is available from OCA.
See Also
Reference
- Doan LT, Martucci WE, Vargo MA, Atreya CE, Anderson KS. Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis. Biochemistry. 2007 Jul 17;46(28):8379-91. Epub 2007 Jun 20. PMID:17580969 doi:10.1021/bi700531r
- Martucci WE, Vargo MA, Anderson KS. Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase. Biochemistry. 2008 Aug 26;47(34):8902-11. Epub 2008 Aug 2. PMID:18672899 doi:10.1021/bi800466z
