1npb

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(New page: 200px<br /><applet load="1npb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npb, resolution 2.50&Aring;" /> '''Crystal structure of...)
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[[Image:1npb.jpg|left|200px]]<br /><applet load="1npb" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1npb.jpg|left|200px]]<br /><applet load="1npb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1npb, resolution 2.50&Aring;" />
caption="1npb, resolution 2.50&Aring;" />
'''Crystal structure of the fosfomycin resistance protein from transposon Tn2921'''<br />
'''Crystal structure of the fosfomycin resistance protein from transposon Tn2921'''<br />
==Overview==
==Overview==
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The crystal structure of fosfomycin resistance protein FosA from, transposon Tn2921 has been established at a resolution of 2.5 A. The, protein crystallized without bound Mn(II) and K+, ions crucial for, efficient catalysis, providing a structure of the apo enzyme. The protein, maintains the three-dimensional domain-swapped arrangement of the paired, betaalphabetabetabeta-motifs observed in the genomically encoded, homologous enzyme from Pseudomonas aeruginosa (PA1129). The basic, architecture of the active site is also maintained, despite the absence of, the catalytically essential Mn(II). However, the absence of K+, which has, been shown to enhance enzymatic activity, appears to contribute to, conformational heterogeneity in the K(+)-binding loops.
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The crystal structure of fosfomycin resistance protein FosA from transposon Tn2921 has been established at a resolution of 2.5 A. The protein crystallized without bound Mn(II) and K+, ions crucial for efficient catalysis, providing a structure of the apo enzyme. The protein maintains the three-dimensional domain-swapped arrangement of the paired betaalphabetabetabeta-motifs observed in the genomically encoded homologous enzyme from Pseudomonas aeruginosa (PA1129). The basic architecture of the active site is also maintained, despite the absence of the catalytically essential Mn(II). However, the absence of K+, which has been shown to enhance enzymatic activity, appears to contribute to conformational heterogeneity in the K(+)-binding loops.
==About this Structure==
==About this Structure==
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1NPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPB OCA].
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1NPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPB OCA].
==Reference==
==Reference==
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[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Armstrong, R.N.]]
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[[Category: Armstrong, R N.]]
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[[Category: Newcomer, M.E.]]
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[[Category: Newcomer, M E.]]
[[Category: Pakhomova, S.]]
[[Category: Pakhomova, S.]]
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[[Category: Rife, C.L.]]
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[[Category: Rife, C L.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: potassium binding loop]]
[[Category: potassium binding loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:27:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:32 2008''

Revision as of 12:08, 21 February 2008


1npb, resolution 2.50Å

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Crystal structure of the fosfomycin resistance protein from transposon Tn2921

Overview

The crystal structure of fosfomycin resistance protein FosA from transposon Tn2921 has been established at a resolution of 2.5 A. The protein crystallized without bound Mn(II) and K+, ions crucial for efficient catalysis, providing a structure of the apo enzyme. The protein maintains the three-dimensional domain-swapped arrangement of the paired betaalphabetabetabeta-motifs observed in the genomically encoded homologous enzyme from Pseudomonas aeruginosa (PA1129). The basic architecture of the active site is also maintained, despite the absence of the catalytically essential Mn(II). However, the absence of K+, which has been shown to enhance enzymatic activity, appears to contribute to conformational heterogeneity in the K(+)-binding loops.

About this Structure

1NPB is a Single protein structure of sequence from Serratia marcescens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of fosfomycin resistance protein FosA from transposon Tn2921., Pakhomova S, Rife CL, Armstrong RN, Newcomer ME, Protein Sci. 2004 May;13(5):1260-5. Epub 2004 Apr 9. PMID:15075406

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