1a7e
From Proteopedia
(New page: 200px<br /><applet load="1a7e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a7e, resolution 1.8Å" /> '''HYDROXOMET MYOHEMERYT...) |
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- | [[Image:1a7e.gif|left|200px]]<br /><applet load="1a7e" size=" | + | [[Image:1a7e.gif|left|200px]]<br /><applet load="1a7e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a7e, resolution 1.8Å" /> | caption="1a7e, resolution 1.8Å" /> | ||
'''HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA'''<br /> | '''HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA'''<br /> | ||
==Overview== | ==Overview== | ||
- | Myohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the | + | Myohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the retractor muscles of marine "peanut" worms. The X-ray crystal structures of two recombinant Themiste zostericola Mhrs are reported to a resolution of 1.8 A. Surprisingly, the met wild-type structure (R = 17.8%) was found to contain chloride bound to Fe2, while coordinated hydroxide was found in the met L103N structure (R = 18.3%). An internal water molecule was also found distal to the Fe-O-Fe center of the mutant protein, forming hydrogen bonds with the coordinated hydroxide and the OD1 atom of Asn-103. This finding is consistent with the kinetic and spectroscopic results reported for the L103N mutant Mhr [Raner, G. M., Martins, L. J., & Ellis, W. R., Jr. (1997) Biochemistry 36, 7037-7043]. Possible roles for the side chain of residue 103 (Leu in wild-type Mhr) in gating ligand binding are also discussed. |
==About this Structure== | ==About this Structure== | ||
- | 1A7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_zostericola Themiste zostericola] with CL and OFO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1A7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_zostericola Themiste zostericola] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=OFO:'>OFO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Themiste zostericola]] | [[Category: Themiste zostericola]] | ||
- | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
- | [[Category: Junior, W | + | [[Category: Junior, W R.Ellis.]] |
- | [[Category: Martins, L | + | [[Category: Martins, L J.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: OFO]] | [[Category: OFO]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:40 2008'' |
Revision as of 09:41, 21 February 2008
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HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA
Overview
Myohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the retractor muscles of marine "peanut" worms. The X-ray crystal structures of two recombinant Themiste zostericola Mhrs are reported to a resolution of 1.8 A. Surprisingly, the met wild-type structure (R = 17.8%) was found to contain chloride bound to Fe2, while coordinated hydroxide was found in the met L103N structure (R = 18.3%). An internal water molecule was also found distal to the Fe-O-Fe center of the mutant protein, forming hydrogen bonds with the coordinated hydroxide and the OD1 atom of Asn-103. This finding is consistent with the kinetic and spectroscopic results reported for the L103N mutant Mhr [Raner, G. M., Martins, L. J., & Ellis, W. R., Jr. (1997) Biochemistry 36, 7037-7043]. Possible roles for the side chain of residue 103 (Leu in wild-type Mhr) in gating ligand binding are also discussed.
About this Structure
1A7E is a Single protein structure of sequence from Themiste zostericola with and as ligands. Full crystallographic information is available from OCA.
Reference
Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution., Martins LJ, Hill CP, Ellis WR Jr, Biochemistry. 1997 Jun 10;36(23):7044-9. PMID:9188702
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