3guz
From Proteopedia
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| - | + | ===Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's=== | |
| - | Description: Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_20059543}}, adds the Publication Abstract to the page | ||
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| + | {{ABSTRACT_PUBMED_20059543}} | ||
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| + | ==About this Structure== | ||
| + | 3GUZ is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GUZ OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:20059543</ref><references group="xtra"/> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Pantoate--beta-alanine ligase]] | ||
| + | [[Category: Chakrabarti, K S.]] | ||
| + | [[Category: Gopal, B.]] | ||
| + | [[Category: Sarma, S P.]] | ||
| + | [[Category: Thakur, K G.]] | ||
| + | [[Category: Atp-binding]] | ||
| + | [[Category: Competitive inhibition]] | ||
| + | [[Category: Cytoplasm]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Non-canonical pantoate binding-site]] | ||
| + | [[Category: Nucleotide-binding]] | ||
| + | [[Category: Pantothenate biosynthesis]] | ||
| + | [[Category: Rossmann fold]] | ||
| + | [[Category: Substrate binding]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 17:22:51 2010'' | ||
Revision as of 15:22, 10 February 2010
Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's
Template:ABSTRACT PUBMED 20059543
About this Structure
3GUZ is a 2 chains structure with sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Chakrabarti KS, Thakur KG, Gopal B, Sarma SP. X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate. FEBS J. 2010 Feb;277(3):697-712. Epub 2010 Jan 4. PMID:20059543 doi:10.1111/j.1742-4658.2009.07515.x
Page seeded by OCA on Wed Feb 10 17:22:51 2010
Categories: Escherichia coli | Pantoate--beta-alanine ligase | Chakrabarti, K S. | Gopal, B. | Sarma, S P. | Thakur, K G. | Atp-binding | Competitive inhibition | Cytoplasm | Ligase | Non-canonical pantoate binding-site | Nucleotide-binding | Pantothenate biosynthesis | Rossmann fold | Substrate binding
