1igw
From Proteopedia
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| - | [[Image:1igw.gif|left|200px]] | + | [[Image:1igw.gif|left|200px]] |
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| - | '''Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli''' | + | {{Structure |
| + | |PDB= 1igw |SIZE=350|CAPTION= <scene name='initialview01'>1igw</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= aceA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IGW is a [ | + | 1IGW 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=1IGW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11526312 11526312] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Isocitrate lyase]] | [[Category: Isocitrate lyase]] | ||
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[[Category: beta barrel]] | [[Category: beta barrel]] | ||
| - | ''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 11:50:11 2008'' |
Revision as of 09:50, 20 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | aceA (Escherichia coli) | ||||||
| Activity: | Isocitrate lyase, with EC number 4.1.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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