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| | [[Image:2pan.jpg|left|200px]] | | [[Image:2pan.jpg|left|200px]] |
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| - | {{Structure
| + | <!-- |
| - | |PDB= 2pan |SIZE=350|CAPTION= <scene name='initialview01'>2pan</scene>, resolution 2.70Å
| + | The line below this paragraph, containing "STRUCTURE_2pan", creates the "Structure Box" on the page. |
| - | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+851'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+851'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+851'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Residue+D+851'>AC4</scene>, <scene name='pdbsite=AC5:Mg+Binding+Site+For+Residue+E+851'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Residue+F+851'>AC6</scene>, <scene name='pdbsite=AC7:Mg+Binding+Site+For+Residue+A+1501'>AC7</scene>, <scene name='pdbsite=AC8:Mg+Binding+Site+For+Residue+B+1501'>AC8</scene>, <scene name='pdbsite=AC9:Mg+Binding+Site+For+Residue+E+1501'>AC9</scene>, <scene name='pdbsite=BC1:Mg+Binding+Site+For+Residue+F+1501'>BC1</scene>, <scene name='pdbsite=BC2:Fad+Binding+Site+For+Residue+A+701'>BC2</scene>, <scene name='pdbsite=BC3:Tdp+Binding+Site+For+Residue+A+801'>BC3</scene>, <scene name='pdbsite=BC4:Dtt+Binding+Site+For+Residue+A+901'>BC4</scene>, <scene name='pdbsite=BC5:Fad+Binding+Site+For+Residue+B+701'>BC5</scene>, <scene name='pdbsite=BC6:Tdp+Binding+Site+For+Residue+B+801'>BC6</scene>, <scene name='pdbsite=BC7:Dtt+Binding+Site+For+Residue+B+901'>BC7</scene>, <scene name='pdbsite=BC8:Fad+Binding+Site+For+Residue+C+701'>BC8</scene>, <scene name='pdbsite=BC9:Tdp+Binding+Site+For+Residue+C+801'>BC9</scene>, <scene name='pdbsite=CC1:Dtt+Binding+Site+For+Residue+C+901'>CC1</scene>, <scene name='pdbsite=CC2:Fad+Binding+Site+For+Residue+D+701'>CC2</scene>, <scene name='pdbsite=CC3:Tdp+Binding+Site+For+Residue+D+801'>CC3</scene>, <scene name='pdbsite=CC4:Dtt+Binding+Site+For+Residue+D+901'>CC4</scene>, <scene name='pdbsite=CC5:Fad+Binding+Site+For+Residue+E+701'>CC5</scene>, <scene name='pdbsite=CC6:Tdp+Binding+Site+For+Residue+E+801'>CC6</scene>, <scene name='pdbsite=CC7:Dtt+Binding+Site+For+Residue+E+901'>CC7</scene>, <scene name='pdbsite=CC8:Fad+Binding+Site+For+Residue+F+701'>CC8</scene>, <scene name='pdbsite=CC9:Tdp+Binding+Site+For+Residue+F+801'>CC9</scene>, <scene name='pdbsite=DC1:Dtt+Binding+Site+For+Residue+F+901'>DC1</scene> and <scene name='pdbsite=DC2:1pe+Binding+Site+For+Residue+A+951'>DC2</scene>
| + | You may change the PDB parameter (which sets the PDB file loaded into the applet) |
| - | |LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene>
| + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tartronate-semialdehyde_synthase Tartronate-semialdehyde synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.47 4.1.1.47] </span>
| + | or leave the SCENE parameter empty for the default display. |
| - | |GENE= gcl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | + | --> |
| - | |DOMAIN= | + | {{STRUCTURE_2pan| PDB=2pan | SCENE= }} |
| - | |RELATEDENTRY=
| + | |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pan OCA], [http://www.ebi.ac.uk/pdbsum/2pan PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pan RCSB]</span>
| + | |
| - | }} | + | |
| | | | |
| | '''Crystal structure of E. coli glyoxylate carboligase''' | | '''Crystal structure of E. coli glyoxylate carboligase''' |
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| | [[Category: Shaanan, B.]] | | [[Category: Shaanan, B.]] |
| | [[Category: Vyazmensky, M.]] | | [[Category: Vyazmensky, M.]] |
| - | [[Category: enzyme]] | + | [[Category: Enzyme]] |
| - | [[Category: fad]] | + | [[Category: Fad]] |
| - | [[Category: glyoxylate carboligase]] | + | [[Category: Glyoxylate carboligase]] |
| - | [[Category: lyase]] | + | [[Category: Lyase]] |
| - | [[Category: thiamin-diphosphate (thdp)]] | + | [[Category: Thimain-dependent enzyme]] |
| - | [[Category: thimain-dependent enzyme]]
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:44:30 2008'' |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:33:39 2008'' | + | |
Thiamine diphosphate (ThDP), a derivative of vitamin B1, is an enzymatic cofactor whose special chemical properties allow it to play critical mechanistic roles in a number of essential metabolic enzymes. It has been assumed that all ThDP-dependent enzymes exploit a polar interaction between a strictly conserved glutamate and the N1' of the ThDP moiety. The crystal structure of glyoxylate carboligase challenges this paradigm by revealing that valine replaces the conserved glutamate. Through kinetic, spectroscopic and site-directed mutagenesis studies, we show that although this extreme change lowers the rate of the initial step of the enzymatic reaction, it ensures efficient progress through subsequent steps. Glyoxylate carboligase thus provides a unique illustration of the fine tuning between catalytic stages imposed during evolution on enzymes catalyzing multistep processes.
Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes., Kaplun A, Binshtein E, Vyazmensky M, Steinmetz A, Barak Z, Chipman DM, Tittmann K, Shaanan B, Nat Chem Biol. 2008 Feb;4(2):113-8. Epub 2008 Jan 6. PMID:18176558
Page seeded by OCA on Sun May 4 12:44:30 2008
