2bkb
From Proteopedia
(New page: 200px<br /> <applet load="2bkb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bkb, resolution 1.70Å" /> '''Q69E-FESOD'''<br />...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BKB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with FE2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BKB OCA]]. | + | 2BKB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with FE2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BKB OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Superoxide dismutase]] | ||
[[Category: Miller, A.F.]] | [[Category: Miller, A.F.]] | ||
[[Category: Rodgers, D.W.]] | [[Category: Rodgers, D.W.]] | ||
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[[Category: superoxide dismutase]] | [[Category: superoxide dismutase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:07:12 2007'' |
Revision as of 12:02, 30 October 2007
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Q69E-FESOD
Overview
Fe-containing superoxide dismutase's active site Fe is coordinated by a, solvent molecule, whose protonation state is coupled to the Fe oxidation, state. Thus, we have proposed that H-bonding between glutamine 69 and this, solvent molecule can strongly influence the redox activity of the Fe in, superoxide dismutase (SOD). We show here that mutation of this Gln to His, subtly alters the active site structure but preserves 30% activity. In, contrast, mutation to Glu otherwise preserves the active site structure, but inactivates the enzyme. Thus, enzyme function correlates not with atom, positions but with residue identity (chemistry), in this case. We observe, strong destabilization of the Q69E-FeSOD oxidized state relative to the, reduced state and intermediate destabilization of oxidized ... [(full description)]
About this Structure
2BKB is a [Single protein] structure of sequence from [Escherichia coli] with FE2 as [ligand]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase., Yikilmaz E, Rodgers DW, Miller AF, Biochemistry. 2006 Jan 31;45(4):1151-61. PMID:16430211
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