2b2k

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[[Image:2b2k.jpg|left|200px]]
[[Image:2b2k.jpg|left|200px]]
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{{Structure
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|PDB= 2b2k |SIZE=350|CAPTION= <scene name='initialview01'>2b2k</scene>, resolution 1.97&Aring;
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The line below this paragraph, containing "STRUCTURE_2b2k", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=EIP:4-HYDROXY-3-METHYL+BUTYL+DIPHOSPHATE'>EIP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2b2k| PDB=2b2k | SCENE= }}
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|RELATEDENTRY=[[1hx3|1HX3]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b2k OCA], [http://www.ebi.ac.uk/pdbsum/2b2k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b2k RCSB]</span>
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}}
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'''structure of Y104F IDI-1 mutant in complex with EIPP'''
'''structure of Y104F IDI-1 mutant in complex with EIPP'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Wouters, J.]]
[[Category: Wouters, J.]]
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[[Category: complex]]
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[[Category: Complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:46:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:00:38 2008''
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Revision as of 16:46, 3 May 2008

Image:2b2k.jpg

Template:STRUCTURE 2b2k

structure of Y104F IDI-1 mutant in complex with EIPP


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.

About this Structure

2B2K is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography., de Ruyck J, Durisotti V, Oudjama Y, Wouters J, J Biol Chem. 2006 Jun 30;281(26):17864-9. Epub 2006 Apr 15. PMID:16617181 Page seeded by OCA on Sat May 3 19:46:21 2008

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