1w4h
From Proteopedia
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[[Image:1w4h.png|left|200px]] | [[Image:1w4h.png|left|200px]] | ||
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{{STRUCTURE_1w4h| PDB=1w4h | SCENE= }} | {{STRUCTURE_1w4h| PDB=1w4h | SCENE= }} | ||
===PERIPHERAL-SUBUNIT FROM MESOPHILIC, THERMOPHILIC AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS=== | ===PERIPHERAL-SUBUNIT FROM MESOPHILIC, THERMOPHILIC AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS=== | ||
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{{ABSTRACT_PUBMED_16168437}} | {{ABSTRACT_PUBMED_16168437}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1w4h]] is a 1 chain structure of [[Dihydrolipoamide acetyltransferase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4H OCA]. | |
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| + | ==See Also== | ||
| + | *[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016168437</ref><references group="xtra"/> |
[[Category: Dihydrolipoyllysine-residue acetyltransferase]] | [[Category: Dihydrolipoyllysine-residue acetyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Ultrafast folding]] | [[Category: Ultrafast folding]] | ||
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Revision as of 02:58, 26 July 2012
Contents |
PERIPHERAL-SUBUNIT FROM MESOPHILIC, THERMOPHILIC AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS
Template:ABSTRACT PUBMED 16168437
About this Structure
1w4h is a 1 chain structure of Dihydrolipoamide acetyltransferase with sequence from Escherichia coli. Full experimental information is available from OCA.
See Also
Reference
- Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR. Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. J Mol Biol. 2005 Oct 21;353(2):427-46. PMID:16168437 doi:10.1016/j.jmb.2005.08.031
