1mkz

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(New page: 200px<br /><applet load="1mkz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mkz, resolution 1.60&Aring;" /> '''Crystal structure of...)
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[[Image:1mkz.jpg|left|200px]]<br /><applet load="1mkz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mkz.jpg|left|200px]]<br /><applet load="1mkz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mkz, resolution 1.60&Aring;" />
caption="1mkz, resolution 1.60&Aring;" />
'''Crystal structure of MoaB protein at 1.6 A resolution.'''<br />
'''Crystal structure of MoaB protein at 1.6 A resolution.'''<br />
==Overview==
==Overview==
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The crystal structure of Escherichia coli MoaB was determined by, multiwavelength anomalous diffraction phasing and refined at 1.6-A, resolution. The molecule displayed a modified Rossman fold. MoaB is, assembled into a hexamer composed of two trimers. The monomers have high, structural similarity with two proteins, MogA and MoeA, from the, molybdenum cofactor synthesis pathway in E. coli, as well as with domains, of mammalian gephyrin and plant Cnx1, which are also involved in, molybdopterin synthesis. Structural comparison between these proteins and, the amino acid conservation patterns revealed a putative active site in, MoaB. The structural analysis of this site allowed to advance several, hypothesis that can be tested in further studies.
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The crystal structure of Escherichia coli MoaB was determined by multiwavelength anomalous diffraction phasing and refined at 1.6-A resolution. The molecule displayed a modified Rossman fold. MoaB is assembled into a hexamer composed of two trimers. The monomers have high structural similarity with two proteins, MogA and MoeA, from the molybdenum cofactor synthesis pathway in E. coli, as well as with domains of mammalian gephyrin and plant Cnx1, which are also involved in molybdopterin synthesis. Structural comparison between these proteins and the amino acid conservation patterns revealed a putative active site in MoaB. The structural analysis of this site allowed to advance several hypothesis that can be tested in further studies.
==About this Structure==
==About this Structure==
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1MKZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MKZ OCA].
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1MKZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKZ OCA].
==Reference==
==Reference==
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[[Category: Edwards, A.]]
[[Category: Edwards, A.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
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[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
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[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Sanishvili, R.]]
[[Category: Sanishvili, R.]]
[[Category: Savchenko, A.]]
[[Category: Savchenko, A.]]
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[[Category: weak anomalous signal]]
[[Category: weak anomalous signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:29:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:15 2008''

Revision as of 11:56, 21 February 2008


1mkz, resolution 1.60Å

Drag the structure with the mouse to rotate

Crystal structure of MoaB protein at 1.6 A resolution.

Overview

The crystal structure of Escherichia coli MoaB was determined by multiwavelength anomalous diffraction phasing and refined at 1.6-A resolution. The molecule displayed a modified Rossman fold. MoaB is assembled into a hexamer composed of two trimers. The monomers have high structural similarity with two proteins, MogA and MoeA, from the molybdenum cofactor synthesis pathway in E. coli, as well as with domains of mammalian gephyrin and plant Cnx1, which are also involved in molybdopterin synthesis. Structural comparison between these proteins and the amino acid conservation patterns revealed a putative active site in MoaB. The structural analysis of this site allowed to advance several hypothesis that can be tested in further studies.

About this Structure

1MKZ is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis., Sanishvili R, Beasley S, Skarina T, Glesne D, Joachimiak A, Edwards A, Savchenko A, J Biol Chem. 2004 Oct 1;279(40):42139-46. Epub 2004 Jul 21. PMID:15269205

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