1nit: Difference between revisions
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'''CRYSTAL STRUCTURE OF ACONITASE WITH TRANS-ACONITATE AND NITROCITRATE BOUND''' | {{Structure | ||
|PDB= 1nit |SIZE=350|CAPTION= <scene name='initialview01'>1nit</scene>, resolution 2.05Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=SF4:IRON/SULFUR CLUSTER'>SF4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF ACONITASE WITH TRANS-ACONITATE AND NITROCITRATE BOUND''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NIT is a [ | 1NIT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIT OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structures of aconitase with trans-aconitate and nitrocitrate bound., Lauble H, Kennedy MC, Beinert H, Stout CD, J Mol Biol. 1994 Apr 8;237(4):437-51. PMID:[http:// | Crystal structures of aconitase with trans-aconitate and nitrocitrate bound., Lauble H, Kennedy MC, Beinert H, Stout CD, J Mol Biol. 1994 Apr 8;237(4):437-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8151704 8151704] | ||
[[Category: Aconitate hydratase]] | [[Category: Aconitate hydratase]] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
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[[Category: lyase(carbon-oxygen)]] | [[Category: lyase(carbon-oxygen)]] | ||
''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 12:57:25 2008'' | ||
Revision as of 13:57, 20 March 2008
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| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aconitate hydratase, with EC number 4.2.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ACONITASE WITH TRANS-ACONITATE AND NITROCITRATE BOUND
OverviewOverview
Crystal structures of mitochondrial aconitase with the inhibitors trans-aconitate and nitrocitrate bound to the [4Fe-4S] cluster have been solved and refined at 2.05 A resolution with R-factors of 0.168 and 0.172, respectively. Crystallization of aconitase with the substrates citrate and cis-aconitate has not been possible because the enzyme turns over and selects enzyme with isocitrate bound into the crystal lattice. Therefore we have analyzed crystal structures of the enzyme complexed with inhibitor analogs of these two substrates. The structure with nitrocitrate bound provides a model for citrate binding. The structure with trans-aconitate bound provides a model for cis-aconitate binding in two ways: Fe4 of the [4Fe-4S] cluster is five-coordinate and the carbon at the C beta position is trigonal. These results allow the model for the reaction mechanism to be extended to all three natural substrates of aconitase. The results support a model in which citrate and isocitrate form similar chelate structures related by 180 degrees rotation about the C alpha-C beta bond while the intermediate cis-aconitate binds in either of two ways (citrate mode or isocitrate mode). In both inhibitor complexes a H2O molecule is also bound to Fe4. In the structure with nitrocitrate bound, partial occupancy of sulfate in the active site is observed accompanied by hydroxyl binding to Fe4. Comparison of the structures with isocitrate, trans-aconitate, nitrocitrate and sulfate bound reveals preferred orientations for the three types of oxygens ligated to Fe4 (carboxyl, hydroxyl and H2O) supporting the proposed roles for His101, Asp165 and His167 in the catalytic mechanism.
About this StructureAbout this Structure
1NIT is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of aconitase with trans-aconitate and nitrocitrate bound., Lauble H, Kennedy MC, Beinert H, Stout CD, J Mol Biol. 1994 Apr 8;237(4):437-51. PMID:8151704
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