3tim: Difference between revisions

Revision as of 13:09, 3 July 2008

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File:3tim.png

Template:STRUCTURE 3tim

THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASETHE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE

Template:ABSTRACT PUBMED 2062827

About this StructureAbout this Structure

3TIM is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase., Wierenga RK, Noble ME, Postma JP, Groendijk H, Kalk KH, Hol WG, Opperdoes FR, Proteins. 1991;10(1):33-49. PMID:2062827

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

OCA

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-[[Image:3tim.jpg|left|200px]]
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 {{STRUCTURE_3tim|  PDB=3tim  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE'''
+===THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE===
-==Overview==
+<!--
-Triosephosphate isomerase has an important loop near the active site which can exist in a "closed" and in an "open" conformation. Here we describe the structural properties of this "flexible" loop observed in two different structures of trypanosomal triosephosphate isomerase. Trypanosomal triosephosphate isomerase, crystallized in the presence of 2.4 M ammonium sulfate, packs as an asymmetric dimer of 54,000 Da in the crystallographic asymmetric unit. Due to different crystal contacts, peptide 167-180 (the flexible loop of subunit-1) is an open conformation, whereas in subunit-2, this peptide (residues 467-480) is in a closed conformation. In the closed conformation, a hydrogen bond exists between the tip of the loop and a well-defined sulfate ion which is bound to the active site of subunit-2. Such an active site sulfate is not present in subunit-1 due to crystal contacts. When the native (2.4 M ammonium sulfate) crystals are transferred to a sulfate-free mother liquor, the flexible loop of subunit-2 adopts the open conformation. From a closed starting model, this open conformation was discovered through molecular dynamics refinement without manual intervention, despite involving C alpha shifts of up to 7 A. The tip of the loop, residues 472, 473, 474, and 475, moves as a rigid body. Our analysis shows that in this crystal form the flexible loop of subunit-2 faces a solvent channel. Therefore the open and the closed conformations of this flexible loop are virtually unaffected by crystal contacts. The actual observed conformation depends only on the absence or presence of a suitable ligand in the active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_2062827}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2062827 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_2062827}}
 ==About this Structure==
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 [[Category: Trypanosoma brucei brucei]]
 [[Category: Wierenga, R K.]]
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