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1a7d

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(New page: 200px<br /><applet load="1a7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a7d, resolution 1.8&Aring;" /> '''CHLOROMET MYOHEMERYTH...)
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[[Image:1a7d.gif|left|200px]]<br /><applet load="1a7d" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a7d, resolution 1.8&Aring;" />
caption="1a7d, resolution 1.8&Aring;" />
'''CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA'''<br />
'''CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA'''<br />
==Overview==
==Overview==
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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., &amp; 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.
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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., &amp; 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==
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1A7D 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 CFO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A7D OCA].
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1A7D 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=CFO:'>CFO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7D OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Themiste zostericola]]
[[Category: Themiste zostericola]]
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[[Category: Hill, C.P.]]
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[[Category: Hill, C P.]]
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[[Category: Junior, W.R.Ellis.]]
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[[Category: Junior, W R.Ellis.]]
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[[Category: Martins, L.J.]]
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[[Category: Martins, L J.]]
[[Category: CFO]]
[[Category: CFO]]
[[Category: CL]]
[[Category: CL]]
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[[Category: oxygen transport]]
[[Category: oxygen transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:39:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:42 2008''

Revision as of 09:41, 21 February 2008


1a7d, resolution 1.8Å

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CHLOROMET 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

1A7D 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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