2pan
From Proteopedia
(New page: 200px<br /><applet load="2pan" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pan, resolution 2.70Å" /> '''Crystal structure of...) |
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caption="2pan, resolution 2.70Å" /> | caption="2pan, resolution 2.70Å" /> | ||
'''Crystal structure of E. coli glyoxylate carboligase'''<br /> | '''Crystal structure of E. coli glyoxylate carboligase'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
| - | 2PAN 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=MG:'>MG</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=TDP:'>TDP</scene>, <scene name='pdbligand=DTT:'>DTT</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PAN OCA]. | + | 2PAN 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=MG:'>MG</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=TDP:'>TDP</scene>, <scene name='pdbligand=DTT:'>DTT</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PAN OCA]. |
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| + | ==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18176558 18176558] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thimain-dependent enzymes]] | [[Category: thimain-dependent enzymes]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:57:42 2008'' |
Revision as of 08:57, 31 January 2008
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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 with , , , and as ligands. Active as Tartronate-semialdehyde synthase, with EC number 4.1.1.47 Known structural/functional Sites: , , , , , , , , , , , , , , , , , , , , , , , , , , , and . 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 Jan 31 10:57:42 2008
