2pan
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[Image:2pan.jpg|left|200px]] | + | [[Image:2pan.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal structure of E. coli glyoxylate carboligase''' | + | {{Structure |
| + | |PDB= 2pan |SIZE=350|CAPTION= <scene name='initialview01'>2pan</scene>, resolution 2.70Å | ||
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> and <scene name='pdbligand=1PE:PENTAETHYLENE GLYCOL'>1PE</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= gcl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of E. coli glyoxylate carboligase''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2PAN is a [ | + | 2PAN 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=2PAN OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18176558 18176558] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 29: | Line 38: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
[[Category: thiamin-diphosphate (thdp)]] | [[Category: thiamin-diphosphate (thdp)]] | ||
| - | [[Category: thimain-dependent | + | [[Category: thimain-dependent enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:10:56 2008'' |
Revision as of 16:11, 20 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , , , , , , , , , , , , , , , and | ||||||
| Ligands: | , , , and | ||||||
| Gene: | gcl (Escherichia coli) | ||||||
| Activity: | Tartronate-semialdehyde synthase, with EC number 4.1.1.47 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of E. coli glyoxylate carboligase
Overview
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.
About this Structure
2PAN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 18:10:56 2008
