2b2k: Difference between revisions

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New page: left|200px<br /><applet load="2b2k" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b2k, resolution 1.97Å" /> '''structure of Y104F I...
 
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[[Image:2b2k.jpg|left|200px]]<br /><applet load="2b2k" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2b2k.jpg|left|200px]]<br /><applet load="2b2k" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2b2k, resolution 1.97&Aring;" />
caption="2b2k, resolution 1.97&Aring;" />
'''structure of Y104F IDI-1 mutant in complex with EIPP'''<br />
'''structure of Y104F IDI-1 mutant in complex with EIPP'''<br />


==Overview==
==Overview==
Isopentenyl-diphosphate (IPP):dimethylallyl diphosphate isomerase is a key, enzyme in the biosynthesis of isoprenoids. The mechanism of the, isomerization reaction involves protonation of the unactivated, carbon-carbon double bond in the substrate, but identity of the acidic, moiety providing the proton is still not clear. Multiple sequence, alignments and geometrical features observed in crystal structures of, complexes with IPP isomerase suggest that Tyr-104 could play an important, role during catalysis. A series of mutants was constructed by directed, mutagenesis and characterized by enzymology. Crystallographic and thermal, denaturation data for Y104A and Y104F mutants were obtained. Those data, demonstrate the importance of residue Tyr-104 for proper folding of, Escherichia coli type I IPP isomerase.
Isopentenyl-diphosphate (IPP):dimethylallyl diphosphate isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate, but identity of the acidic moiety providing the proton is still not clear. Multiple sequence alignments and geometrical features observed in crystal structures of complexes with IPP isomerase suggest that Tyr-104 could play an important role during catalysis. A series of mutants was constructed by directed mutagenesis and characterized by enzymology. Crystallographic and thermal denaturation data for Y104A and Y104F mutants were obtained. Those data demonstrate the importance of residue Tyr-104 for proper folding of Escherichia coli type I IPP isomerase.


==About this Structure==
==About this Structure==
2B2K 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 MN, MG and EIP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B2K OCA].  
2B2K 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=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EIP:'>EIP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B2K OCA].  


==Reference==
==Reference==
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[[Category: complex]]
[[Category: complex]]


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