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1zxj

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(New page: 200px<br /><applet load="1zxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zxj, resolution 2.80&Aring;" /> '''Crystal structure of...)
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[[Image:1zxj.gif|left|200px]]<br /><applet load="1zxj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zxj.gif|left|200px]]<br /><applet load="1zxj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zxj, resolution 2.80&Aring;" />
caption="1zxj, resolution 2.80&Aring;" />
'''Crystal structure of the hypthetical Mycoplasma protein, MPN555'''<br />
'''Crystal structure of the hypthetical Mycoplasma protein, MPN555'''<br />
==Overview==
==Overview==
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The crystal structure of the hypothetical protein MPN555 from Mycoplasma, pneumoniae (gi|1673958) has been determined to a resolution of 2.8, Angstrom using anomalous diffraction data at the Se-peak wavelength., Structure determination revealed a mostly alpha-helical protein with a, three-lobed shape. The three lobes or fingers delineate a central binding, groove and additional grooves between lobes 1 and 3 and between lobes 2, and 3. For one of the molecules in the asymmetric unit, the central, binding pocket was filled with a peptide from the uncleaved N-terminal, affinity tag. The MPN555 structure has structural homology to two, bacterial chaperone proteins: SurA and trigger factor from Escherichia, coli. The structural data and the homology to other chaperone proteins, suggests an involvement in protein folding as a molecular chaperone for, MPN555.
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The crystal structure of the hypothetical protein MPN555 from Mycoplasma pneumoniae (gi|1673958) has been determined to a resolution of 2.8 Angstrom using anomalous diffraction data at the Se-peak wavelength. Structure determination revealed a mostly alpha-helical protein with a three-lobed shape. The three lobes or fingers delineate a central binding groove and additional grooves between lobes 1 and 3 and between lobes 2 and 3. For one of the molecules in the asymmetric unit, the central binding pocket was filled with a peptide from the uncleaved N-terminal affinity tag. The MPN555 structure has structural homology to two bacterial chaperone proteins: SurA and trigger factor from Escherichia coli. The structural data and the homology to other chaperone proteins suggests an involvement in protein folding as a molecular chaperone for MPN555.
==About this Structure==
==About this Structure==
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1ZXJ 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=1ZXJ OCA].
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1ZXJ 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=1ZXJ OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Aono, S.]]
[[Category: Aono, S.]]
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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: Kim, S.H.]]
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[[Category: Kim, S H.]]
[[Category: Schulze-Gahmen, U.]]
[[Category: Schulze-Gahmen, U.]]
[[Category: Shengfeng, C.]]
[[Category: Shengfeng, C.]]
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[[Category: tri-lobal structure]]
[[Category: tri-lobal structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:43:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:05 2008''

Revision as of 14:20, 21 February 2008


1zxj, resolution 2.80Å

Drag the structure with the mouse to rotate

Crystal structure of the hypthetical Mycoplasma protein, MPN555

Overview

The crystal structure of the hypothetical protein MPN555 from Mycoplasma pneumoniae (gi|1673958) has been determined to a resolution of 2.8 Angstrom using anomalous diffraction data at the Se-peak wavelength. Structure determination revealed a mostly alpha-helical protein with a three-lobed shape. The three lobes or fingers delineate a central binding groove and additional grooves between lobes 1 and 3 and between lobes 2 and 3. For one of the molecules in the asymmetric unit, the central binding pocket was filled with a peptide from the uncleaved N-terminal affinity tag. The MPN555 structure has structural homology to two bacterial chaperone proteins: SurA and trigger factor from Escherichia coli. The structural data and the homology to other chaperone proteins suggests an involvement in protein folding as a molecular chaperone for MPN555.

About this Structure

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

Reference

Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function., Schulze-Gahmen U, Aono S, Chen S, Yokota H, Kim R, Kim SH, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1343-7. Epub 2005, Sep 28. PMID:16204885

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