2c5b

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{{Seed}}
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{{STRUCTURE_2c5b| PDB=2c5b | SCENE= }}
{{STRUCTURE_2c5b| PDB=2c5b | SCENE= }}
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'''X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 2'DEOXY-5'DEOXY-FLUOROADENOSINE.'''
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===X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 2'DEOXY-5'DEOXY-FLUOROADENOSINE.===
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==Overview==
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The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C-F bond. We now report that the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C-F bond formation.
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The line below this paragraph, {{ABSTRACT_PUBMED_16604208}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16604208 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16604208}}
==About this Structure==
==About this Structure==
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[[Category: Streptomyces cattleya]]
[[Category: Streptomyces cattleya]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:16:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:35:41 2008''

Revision as of 10:35, 29 July 2008

Image:2c5b.png

Template:STRUCTURE 2c5b

X-RAY CRYSTAL STRUCTURE OF 5'-FLUORODEOXYADENOSINE SYNTHASE FROM STREPTOMYCES CATTLEYA COMPLEXED WITH 2'DEOXY-5'DEOXY-FLUOROADENOSINE.

Template:ABSTRACT PUBMED 16604208

About this Structure

2C5B is a Single protein structure of sequence from Streptomyces cattleya. Full crystallographic information is available from OCA.

Reference

Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates., Cobb SL, Deng H, McEwan AR, Naismith JH, O'Hagan D, Robinson DA, Org Biomol Chem. 2006 Apr 21;4(8):1458-60. Epub 2006 Mar 8. PMID:16604208

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