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4kl9

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'''Unreleased structure'''
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{{STRUCTURE_4kl9| PDB=4kl9 | SCENE= }}
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===Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in the space group C2===
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{{ABSTRACT_PUBMED_24210757}}
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The entry 4kl9 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/DYR_MYCTU DYR_MYCTU]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
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Authors: Dias, M.V.B, Tyrakis, P., Blundell, T.L.
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==About this Structure==
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[[4kl9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KL9 OCA].
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Description: Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in the space group C2
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==Reference==
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<ref group="xtra">PMID:024210757</ref><references group="xtra"/><references/>
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[[Category: Dihydrofolate reductase]]
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[[Category: Blundell, T L.]]
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[[Category: Dias, M V.B]]
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[[Category: Tyrakis, P.]]
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[[Category: Oxidoreductase]]
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[[Category: Reductase]]

Revision as of 10:17, 25 December 2013

Template:STRUCTURE 4kl9

Contents

Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in the space group C2

Template:ABSTRACT PUBMED 24210757

Function

[DYR_MYCTU] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

About this Structure

4kl9 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Dias MV, Tyrakis P, Domingues RR, Leme AF, Blundell TL. Mycobacterium tuberculosis Dihydrofolate Reductase Reveals Two Conformational States and a Possible Low Affinity Mechanism to Antifolate Drugs. Structure. 2013 Nov 6. pii: S0969-2126(13)00395-X. doi:, 10.1016/j.str.2013.09.022. PMID:24210757 doi:http://dx.doi.org/10.1016/j.str.2013.09.022

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OCA

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