1e7p

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(New page: 200px<br /> <applet load="1e7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e7p, resolution 3.10&Aring;" /> '''QUINOL:FUMARATE RED...)
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==About this Structure==
==About this Structure==
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1E7P is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]] with NA, HEM, FES, F3S, SF4, FAD, MLA and LMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E7P OCA]].
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1E7P is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]] with NA, HEM, FES, F3S, SF4, FAD, MLA and LMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]]. Structure known Active Sites: FA1, FA2, FA3, FA4, FS1, FS2, FS3, FS4, FS5, FS6, FS7, FS8, FS9, FSA, FSB, FSC, HE1, HE2, HE3 and HE4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E7P OCA]].
==Reference==
==Reference==
A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction., Lancaster CR, Gross R, Simon J, Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11248702 11248702]
A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction., Lancaster CR, Gross R, Simon J, Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11248702 11248702]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Succinate dehydrogenase]]
[[Category: Wolinella succinogenes]]
[[Category: Wolinella succinogenes]]
[[Category: Lancaster, C.R.D.]]
[[Category: Lancaster, C.R.D.]]
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[[Category: succinate dehydrogenase]]
[[Category: succinate dehydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:14:44 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:03:22 2007''

Revision as of 08:58, 30 October 2007


1e7p, resolution 3.10Å

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QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

Overview

Quinol:fumarate reductase (QFR) is a membrane protein complex that couples, the reduction of fumarate to succinate to the oxidation of quinol to, quinone. Previously, the crystal structure of QFR from Wolinella, succinogenes was determined based on two different crystal forms, and the, site of fumarate binding in the flavoprotein subunit A of the enzyme was, located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kroger, A., Auer, M., & Michel, H. (1999) Nature 402, 377--385]., Here we describe the structure of W. succinogenes QFR based on a third, crystal form and refined at 3.1 A resolution. Compared with the previous, crystal forms, the capping domain is rotated in this structure by, approximately 14 degrees relative to the FAD-binding domain. As a, ... [(full description)]

About this Structure

1E7P is a [Protein complex] structure of sequences from [Wolinella succinogenes] with NA, HEM, FES, F3S, SF4, FAD, MLA and LMT as [ligands]. Active as [Succinate dehydrogenase], with EC number [1.3.99.1]. Structure known Active Sites: FA1, FA2, FA3, FA4, FS1, FS2, FS3, FS4, FS5, FS6, FS7, FS8, FS9, FSA, FSB, FSC, HE1, HE2, HE3 and HE4. Full crystallographic information is available from [OCA].

Reference

A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction., Lancaster CR, Gross R, Simon J, Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:11248702

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