1c97

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[[Image:1c97.gif|left|200px]]
[[Image:1c97.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1c97 |SIZE=350|CAPTION= <scene name='initialview01'>1c97</scene>, resolution 1.98&Aring;
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The line below this paragraph, containing "STRUCTURE_1c97", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ICT:ISOCITRIC+ACID'>ICT</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1c97| PDB=1c97 | SCENE= }}
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|RELATEDENTRY=[[1c96|1C96]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c97 OCA], [http://www.ebi.ac.uk/pdbsum/1c97 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c97 RCSB]</span>
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}}
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'''S642A:ISOCITRATE COMPLEX OF ACONITASE'''
'''S642A:ISOCITRATE COMPLEX OF ACONITASE'''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:29:01 2008''
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Revision as of 09:29, 2 May 2008

Image:1c97.gif

Template:STRUCTURE 1c97

S642A:ISOCITRATE COMPLEX OF ACONITASE


Overview

The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.

About this Structure

1C97 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex., Lloyd SJ, Lauble H, Prasad GS, Stout CD, Protein Sci. 1999 Dec;8(12):2655-62. PMID:10631981 Page seeded by OCA on Fri May 2 12:29:01 2008

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