1in0

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(New page: 200px<br /><applet load="1in0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1in0, resolution 2.14&Aring;" /> '''YAJQ PROTEIN (HI1034...)
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'''YAJQ PROTEIN (HI1034)'''<br />
'''YAJQ PROTEIN (HI1034)'''<br />
==Overview==
==Overview==
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A hypothetical protein encoded by the gene YajQ of Haemophilus influenzae, was selected, as part of a structural genomics project, for X-ray, crystallographic structure determination and analysis to assist with the, functional assignment. The protein is present in most bacteria, but not in, archaea or eukaryotes. The amino acid sequence has no homology to that of, other proteins. The YajQ protein was cloned, expressed, and the crystal, structure determined at 2.1-A resolution by applying the multiwavelength, anomalous dispersion method to a mercury derivative. The polypeptide chain, is folded into two domains with identical folding topology. Each domain, has a four-stranded antiparallel beta-sheet flanked on one side by two, alpha-helices. This structural motif is a characteristic feature of many, RNA-binding proteins. The tetrameric structure observed in the crystal, suggests a possibility of binding two stretches of double-stranded nucleic, acid.
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A hypothetical protein encoded by the gene YajQ of Haemophilus influenzae was selected, as part of a structural genomics project, for X-ray crystallographic structure determination and analysis to assist with the functional assignment. The protein is present in most bacteria, but not in archaea or eukaryotes. The amino acid sequence has no homology to that of other proteins. The YajQ protein was cloned, expressed, and the crystal structure determined at 2.1-A resolution by applying the multiwavelength anomalous dispersion method to a mercury derivative. The polypeptide chain is folded into two domains with identical folding topology. Each domain has a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices. This structural motif is a characteristic feature of many RNA-binding proteins. The tetrameric structure observed in the crystal suggests a possibility of binding two stretches of double-stranded nucleic acid.
==About this Structure==
==About this Structure==
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1IN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with HG, NA and MMC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IN0 OCA].
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1IN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=MMC:'>MMC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IN0 OCA].
==Reference==
==Reference==
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Gilliland, G.L.]]
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[[Category: Gilliland, G L.]]
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[[Category: S2F, Structure.2.Function.Project.]]
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[[Category: S2F, Structure 2.Function Project.]]
[[Category: Teplyakov, A.]]
[[Category: Teplyakov, A.]]
[[Category: HG]]
[[Category: HG]]
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[[Category: structure 2 function project]]
[[Category: structure 2 function project]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:30:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:29 2008''

Revision as of 11:13, 21 February 2008


1in0, resolution 2.14Å

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YAJQ PROTEIN (HI1034)

Overview

A hypothetical protein encoded by the gene YajQ of Haemophilus influenzae was selected, as part of a structural genomics project, for X-ray crystallographic structure determination and analysis to assist with the functional assignment. The protein is present in most bacteria, but not in archaea or eukaryotes. The amino acid sequence has no homology to that of other proteins. The YajQ protein was cloned, expressed, and the crystal structure determined at 2.1-A resolution by applying the multiwavelength anomalous dispersion method to a mercury derivative. The polypeptide chain is folded into two domains with identical folding topology. Each domain has a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices. This structural motif is a characteristic feature of many RNA-binding proteins. The tetrameric structure observed in the crystal suggests a possibility of binding two stretches of double-stranded nucleic acid.

About this Structure

1IN0 is a Single protein structure of sequence from Haemophilus influenzae with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains., Teplyakov A, Obmolova G, Bir N, Reddy P, Howard AJ, Gilliland GL, J Struct Funct Genomics. 2003;4(1):1-9. PMID:12943362

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