1b0k: Difference between revisions

Revision as of 12:50, 21 February 2008

S642A:FLUOROCITRATE COMPLEX OF ACONITASE

OverviewOverview

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 StructureAbout this Structure

1B0K is a Single protein structure of sequence from Sus scrofa with , and as ligands. This structure supersedes the now removed PDB entry 1AS9. Active as Aconitate hydratase, with EC number 4.2.1.3 Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 11:50:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1b0k.jpg|left|200px]]<br /><applet load="1b0k" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b0k.jpg|left|200px]]<br /><applet load="1b0k" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b0k, resolution 2.50&Aring;" />
 '''S642A:FLUOROCITRATE COMPLEX OF ACONITASE'''<br />
 ==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 --&gt; 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.
+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 --&gt; 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==
-B0K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with FLC, SF4 and O as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1AS9. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B0K OCA].
+B0K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=FLC:'>FLC</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=O:'>O</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1AS9. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0K OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Sus scrofa]]
 [[Category: Lauble, H.]]
-[[Category: Lloyd, S.J.]]
+[[Category: Lloyd, S J.]]
-[[Category: Prasad, G.S.]]
+[[Category: Prasad, G S.]]
-[[Category: Stout, C.D.]]
+[[Category: Stout, C D.]]
 [[Category: FLC]]
 [[Category: O]]
@@ Line 27: / Line 27: @@
 [[Category: tricarboxylic acid cycle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:15:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:13 2008''