1igw
From Proteopedia
(New page: 200px<br /><applet load="1igw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1igw, resolution 2.1Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1igw.gif|left|200px]]<br /><applet load="1igw" size=" | + | [[Image:1igw.gif|left|200px]]<br /><applet load="1igw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1igw, resolution 2.1Å" /> | caption="1igw, resolution 2.1Å" /> | ||
'''Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli'''<br /> | '''Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enzymes of the glyoxylate-bypass pathway are potential targets for the | + | Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 A resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle. |
==About this Structure== | ==About this Structure== | ||
| - | 1IGW 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 HG, MG and PYR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_lyase Isocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.1 4.1.3.1] Full crystallographic information is available from [http:// | + | 1IGW 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=HG:'>HG</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PYR:'>PYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_lyase Isocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.1 4.1.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IGW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Isocitrate lyase]] | [[Category: Isocitrate lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abeysinghe, I | + | [[Category: Abeysinghe, I S.B.]] |
| - | [[Category: Baker, P | + | [[Category: Baker, P J.]] |
[[Category: Barynin, V.]] | [[Category: Barynin, V.]] | ||
| - | [[Category: Britton, K | + | [[Category: Britton, K L.]] |
[[Category: Diehl, P.]] | [[Category: Diehl, P.]] | ||
| - | [[Category: Langridge, S | + | [[Category: Langridge, S J.]] |
| - | [[Category: McFadden, B | + | [[Category: McFadden, B A.]] |
| - | [[Category: Rice, D | + | [[Category: Rice, D W.]] |
| - | [[Category: Sedelnikova, S | + | [[Category: Sedelnikova, S E.]] |
| - | [[Category: Stillman, T | + | [[Category: Stillman, T J.]] |
[[Category: Weeradechapon, K.]] | [[Category: Weeradechapon, K.]] | ||
[[Category: HG]] | [[Category: HG]] | ||
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[[Category: beta barrel]] | [[Category: beta barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:41 2008'' |
Revision as of 11:11, 21 February 2008
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Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli
Overview
Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 A resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle.
About this Structure
1IGW is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Isocitrate lyase, with EC number 4.1.3.1 Full crystallographic information is available from OCA.
Reference
The structure and domain organization of Escherichia coli isocitrate lyase., Britton KL, Abeysinghe IS, Baker PJ, Barynin V, Diehl P, Langridge SJ, McFadden BA, Sedelnikova SE, Stillman TJ, Weeradechapon K, Rice DW, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1209-18. Epub 2001, Aug 23. PMID:11526312
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