1pa4

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(New page: 200px<br /><applet load="1pa4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pa4" /> '''Solution structure of a putative ribosome-bi...)
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[[Image:1pa4.gif|left|200px]]<br /><applet load="1pa4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pa4.gif|left|200px]]<br /><applet load="1pa4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pa4" />
caption="1pa4" />
'''Solution structure of a putative ribosome-binding factor from Mycoplasma pneumoniae (MPN156)'''<br />
'''Solution structure of a putative ribosome-binding factor from Mycoplasma pneumoniae (MPN156)'''<br />
==Overview==
==Overview==
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The solution structure of MPN156, a ribosome-binding factor A (RBFA), protein family member from Mycoplasma pneumoniae, is presented. The, structure, solved by nuclear magnetic resonance, has a type II KH fold, typical of RNA binding proteins. Despite only approximately 20% sequence, identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison, demonstrates that many of the conserved residues correspond to conserved, elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of, amino acids in the two proteins. Implications of these discrepancies for, sequence based structural modeling are discussed.
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The solution structure of MPN156, a ribosome-binding factor A (RBFA) protein family member from Mycoplasma pneumoniae, is presented. The structure, solved by nuclear magnetic resonance, has a type II KH fold typical of RNA binding proteins. Despite only approximately 20% sequence identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison demonstrates that many of the conserved residues correspond to conserved elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of amino acids in the two proteins. Implications of these discrepancies for sequence based structural modeling are discussed.
==About this Structure==
==About this Structure==
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1PA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_pneumoniae Mycoplasma pneumoniae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PA4 OCA].
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1PA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_pneumoniae Mycoplasma pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PA4 OCA].
==Reference==
==Reference==
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[[Category: Mycoplasma pneumoniae]]
[[Category: Mycoplasma pneumoniae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Pelton, J.G.]]
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[[Category: Pelton, J G.]]
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[[Category: Rubin, S.M.]]
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[[Category: Rubin, S M.]]
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[[Category: Wemmer, D.E.]]
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[[Category: Wemmer, D E.]]
[[Category: Yokota, H.]]
[[Category: Yokota, H.]]
[[Category: berkeley structural genomics center]]
[[Category: berkeley structural genomics center]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:37:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:46 2008''

Revision as of 12:26, 21 February 2008


1pa4

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Solution structure of a putative ribosome-binding factor from Mycoplasma pneumoniae (MPN156)

Overview

The solution structure of MPN156, a ribosome-binding factor A (RBFA) protein family member from Mycoplasma pneumoniae, is presented. The structure, solved by nuclear magnetic resonance, has a type II KH fold typical of RNA binding proteins. Despite only approximately 20% sequence identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison demonstrates that many of the conserved residues correspond to conserved elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of amino acids in the two proteins. Implications of these discrepancies for sequence based structural modeling are discussed.

About this Structure

1PA4 is a Single protein structure of sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA.

Reference

Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog., Rubin SM, Pelton JG, Yokota H, Kim R, Wemmer DE, J Struct Funct Genomics. 2003;4(4):235-43. PMID:15185964

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