1mkz

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[[Image:1mkz.jpg|left|200px]]<br /><applet load="1mkz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mkz.jpg|left|200px]]
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caption="1mkz, resolution 1.60&Aring;" />
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'''Crystal structure of MoaB protein at 1.6 A resolution.'''<br />
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{{Structure
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|PDB= 1mkz |SIZE=350|CAPTION= <scene name='initialview01'>1mkz</scene>, resolution 1.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY=
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|GENE= MoaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of MoaB protein at 1.6 A resolution.'''
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==Overview==
==Overview==
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==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 <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].
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1MKZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKZ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15269205 15269205]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15269205 15269205]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: mad]]
[[Category: mad]]
[[Category: mcsg]]
[[Category: mcsg]]
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[[Category: midwest center for structural genomics]]
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[[Category: midwest center for structural genomic]]
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[[Category: molybdopterin synthesis ]]
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[[Category: molybdopterin synthesis]]
[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: weak anomalous signal]]
[[Category: weak anomalous signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:44:46 2008''

Revision as of 10:44, 20 March 2008


PDB ID 1mkz

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: and
Gene: MoaB (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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. 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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