1ei1

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[[Image:1ei1.gif|left|200px]]<br /><applet load="1ei1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ei1.gif|left|200px]]
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caption="1ei1, resolution 2.3&Aring;" />
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'''DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER'''<br />
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{{Structure
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|PDB= 1ei1 |SIZE=350|CAPTION= <scene name='initialview01'>1ei1</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3]
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|GENE=
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}}
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'''DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EI1 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>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI1 OCA].
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1EI1 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=1EI1 OCA].
==Reference==
==Reference==
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Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center., Brino L, Urzhumtsev A, Mousli M, Bronner C, Mitschler A, Oudet P, Moras D, J Biol Chem. 2000 Mar 31;275(13):9468-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10734094 10734094]
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Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center., Brino L, Urzhumtsev A, Mousli M, Bronner C, Mitschler A, Oudet P, Moras D, J Biol Chem. 2000 Mar 31;275(13):9468-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10734094 10734094]
[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: dimer]]
[[Category: dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:51 2008''

Revision as of 08:55, 20 March 2008

Image:1ei1.gif


PDB ID 1ei1

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: , and
Activity: DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3
Coordinates: save as pdb, mmCIF, xml



DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER


Overview

DNA-gyrase exhibits an unusual ATP-binding site that is formed as a result of gyrase B subunit dimerization, a structural transition that is also essential for DNA capture during the topoisomerization cycle. Previous structural studies on Escherichia coli DNA-gyrase B revealed that dimerization is the result of a polypeptidic exchange involving the N-terminal 14 amino acids. To provide experimental data that dimerization is critical for ATPase activity and enzyme turnover, we generated mutants with reduced dimerization by mutating the two most conserved residues of the GyrB N-terminal arm (Tyr-5 and Ile-10 residues). Our data demonstrate that the hydrophobic Ile-10 residue plays an important role in enzyme dimerization and the nucleotide-protein contact mediated by Tyr-5 side chain residue helps the dimerization process. Analysis of ATPase activities of mutant proteins provides evidence that dimerization enhances the ATP-hydrolysis turnover. The structure of the Y5S mutant of the N-terminal 43-kDa fragment of E. coli DNA GyrB subunit indicates that Tyr-5 residue provides a scaffold for the ATP-hydrolysis center. We describe a channel formed at the dimer interface that provides a structural mechanism to allow reactive water molecules to access the gamma-phosphate group of the bound ATP molecule. Together, these results demonstrate that dimerization strongly contributes to the folding and stability of the catalytic site for ATP hydrolysis. A role for the essential Mg(2+) ion for the orientation of the phosphate groups of the bound nucleotide inside the reactive pocket was also uncovered by superposition of the 5'-adenylyl beta-gamma-imidodiphosphate (ADPNP) wild-type structure to the salt-free ADPNP structure.

About this Structure

1EI1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center., Brino L, Urzhumtsev A, Mousli M, Bronner C, Mitschler A, Oudet P, Moras D, J Biol Chem. 2000 Mar 31;275(13):9468-75. PMID:10734094

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