1qhq

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(New page: 200px<br /><applet load="1qhq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qhq, resolution 1.55&Aring;" /> '''AURACYANIN, A BLUE C...)
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'''AURACYANIN, A BLUE COPPER PROTEIN FROM THE GREEN THERMOPHILIC PHOTOSYNTHETIC BACTERIUM CHLOROFLEXUS AURANTIACUS'''<br />
'''AURACYANIN, A BLUE COPPER PROTEIN FROM THE GREEN THERMOPHILIC PHOTOSYNTHETIC BACTERIUM CHLOROFLEXUS AURANTIACUS'''<br />
==Overview==
==Overview==
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Auracyanin B, one of two similar blue copper proteins produced by the, thermophilic green non-sulfur photosynthetic bacterium Chloroflexus, aurantiacus, crystallizes in space group P6(4)22 (a=b=115.7 A, c=54.6 A)., The structure was solved using multiple wavelength anomalous dispersion, data recorded about the CuK absorption edge, and was refined at 1.55 A, resolution. The molecular model comprises 139 amino acid residues, one Cu, 247 H(2)O molecules, one Cl(-) and two SO(4)(2-). The final residual and, estimated standard uncertainties are R=0.198, ESU=0.076 A for atomic, coordinates and ESU=0.05 A for Cu---ligand bond lengths, respectively. The, auracyanin B molecule has a standard cupredoxin fold. With the exception, of an additional N-terminal strand, the molecule is very similar to that, of the bacterial cupredoxin, azurin. As in other cupredoxins, one of the, Cu ligands lies on strand 4 of the polypeptide, and the other three lie, along a large loop between strands 7 and 8. The Cu site geometry is, discussed with reference to the amino acid spacing between the latter, three ligands. The crystallographically characterized Cu-binding domain of, auracyanin B is probably tethered to the periplasmic side of the, cytoplasmic membrane by an N-terminal tail that exhibits significant, sequence identity with known tethers in several other membrane-associated, electron-transfer proteins.
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Auracyanin B, one of two similar blue copper proteins produced by the thermophilic green non-sulfur photosynthetic bacterium Chloroflexus aurantiacus, crystallizes in space group P6(4)22 (a=b=115.7 A, c=54.6 A). The structure was solved using multiple wavelength anomalous dispersion data recorded about the CuK absorption edge, and was refined at 1.55 A resolution. The molecular model comprises 139 amino acid residues, one Cu, 247 H(2)O molecules, one Cl(-) and two SO(4)(2-). The final residual and estimated standard uncertainties are R=0.198, ESU=0.076 A for atomic coordinates and ESU=0.05 A for Cu---ligand bond lengths, respectively. The auracyanin B molecule has a standard cupredoxin fold. With the exception of an additional N-terminal strand, the molecule is very similar to that of the bacterial cupredoxin, azurin. As in other cupredoxins, one of the Cu ligands lies on strand 4 of the polypeptide, and the other three lie along a large loop between strands 7 and 8. The Cu site geometry is discussed with reference to the amino acid spacing between the latter three ligands. The crystallographically characterized Cu-binding domain of auracyanin B is probably tethered to the periplasmic side of the cytoplasmic membrane by an N-terminal tail that exhibits significant sequence identity with known tethers in several other membrane-associated electron-transfer proteins.
==About this Structure==
==About this Structure==
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1QHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus] with CU, CL and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QHQ OCA].
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1QHQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHQ OCA].
==Reference==
==Reference==
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[[Category: Chloroflexus aurantiacus]]
[[Category: Chloroflexus aurantiacus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Blankenship, R.E.]]
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[[Category: Blankenship, R E.]]
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[[Category: Bond, C.S.]]
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[[Category: Bond, C S.]]
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[[Category: Freeman, H.C.]]
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[[Category: Freeman, H C.]]
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[[Category: Guss, J.M.]]
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[[Category: Guss, J M.]]
[[Category: Maher, M.]]
[[Category: Maher, M.]]
[[Category: Selvaraj, F.]]
[[Category: Selvaraj, F.]]
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[[Category: Wilce, M.C.J.]]
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[[Category: Wilce, M C.J.]]
[[Category: Willingham, K.]]
[[Category: Willingham, K.]]
[[Category: CL]]
[[Category: CL]]
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[[Category: thermophile]]
[[Category: thermophile]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:42 2008''

Revision as of 12:39, 21 February 2008


1qhq, resolution 1.55Å

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AURACYANIN, A BLUE COPPER PROTEIN FROM THE GREEN THERMOPHILIC PHOTOSYNTHETIC BACTERIUM CHLOROFLEXUS AURANTIACUS

Overview

Auracyanin B, one of two similar blue copper proteins produced by the thermophilic green non-sulfur photosynthetic bacterium Chloroflexus aurantiacus, crystallizes in space group P6(4)22 (a=b=115.7 A, c=54.6 A). The structure was solved using multiple wavelength anomalous dispersion data recorded about the CuK absorption edge, and was refined at 1.55 A resolution. The molecular model comprises 139 amino acid residues, one Cu, 247 H(2)O molecules, one Cl(-) and two SO(4)(2-). The final residual and estimated standard uncertainties are R=0.198, ESU=0.076 A for atomic coordinates and ESU=0.05 A for Cu---ligand bond lengths, respectively. The auracyanin B molecule has a standard cupredoxin fold. With the exception of an additional N-terminal strand, the molecule is very similar to that of the bacterial cupredoxin, azurin. As in other cupredoxins, one of the Cu ligands lies on strand 4 of the polypeptide, and the other three lie along a large loop between strands 7 and 8. The Cu site geometry is discussed with reference to the amino acid spacing between the latter three ligands. The crystallographically characterized Cu-binding domain of auracyanin B is probably tethered to the periplasmic side of the cytoplasmic membrane by an N-terminal tail that exhibits significant sequence identity with known tethers in several other membrane-associated electron-transfer proteins.

About this Structure

1QHQ is a Single protein structure of sequence from Chloroflexus aurantiacus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of auracyanin, a "blue" copper protein from the green thermophilic photosynthetic bacterium Chloroflexus aurantiacus., Bond CS, Blankenship RE, Freeman HC, Guss JM, Maher MJ, Selvaraj FM, Wilce MC, Willingham KM, J Mol Biol. 2001 Feb 9;306(1):47-67. PMID:11178893

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