1tri: Difference between revisions

Revision as of 14:02, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tri.png

Template:STRUCTURE 1tri

THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOPTHE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP

Template:ABSTRACT PUBMED 16100954

About this StructureAbout this Structure

1TRI is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop., Borchert TV, Abagyan R, Kishan KV, Zeelen JP, Wierenga RK, Structure. 1993 Nov 15;1(3):205-13. PMID:16100954

Page seeded by OCA on Mon Jul 28 14:02:56 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1tri.gif|left|200px]]
+{{Seed}}
+[[Image:1tri.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1tri|  PDB=1tri  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP'''
+===THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP===
-==Overview==
+<!--
-BACKGROUND: The triosephosphate isomerase (TIM) fold is found in several different classes of enzymes, most of which are oligomers; TIM itself always functions as a very tight dimer. It has recently been shown that a monomeric form of TIM ('monoTIM') can be constructed by replacing a 15-residue interface loop, loop-3, with an eight-residue fragment; modelling suggests that this should result in a short strain-free turn, resulting in the subsequent helix, helix-A3, having an additional turn at its amino terminus. RESULTS: The crystal structure of monoTIM shows that it retains the characteristic TIM-barrel (betaalpha)8-fold and that the new loop has a structure very close to that predicted. Two other interface loops, loop-1 and loop-4, which contain the active site residues Lys13 and His95, respectively, show significant changes in structure in monoTIM compared with dimeric wild-type TIM. CONCLUSION: The observed structural differences between monoTIM and wild-type TIM indicate that the dimeric appearance of TIM determines the location and conformation of two of the four catalytic residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_16100954}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16100954 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16100954}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Trypanosoma brucei brucei]]
 [[Category: Wierenga, R K.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:17:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:02:56 2008''