ORBi: Maes Dominique - The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures

Reference : The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a com...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/19823

Title :	The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures
Language :	English
Author, co-author :	Maes, Dominique [Vrije Universiteit Brussel > Vlaams Interuniversitair Instituut voor Biotechnologie > > >]
	Zeelen, Johan P. [European Molecular Biology Laboratory > > > >]
	Thanki, Narmada [European Molecular Biology Laboratory > > > >]
	Beaucamp, Nicola [Universität Regensburg > Institut für Biophysik und physikalische Biochemie > > >]
	Alvarez, Marco [> >]
	Thi, Minh Hoa Dao [Vrije Universiteit Brussel > Vlaams Interuniversitair Instituut voor Biotechnologie > > >]
	Backmann, Jan [Vrije Universiteit Brussel > Vlaams Interuniversitair Instituut voor Biotechnologie > > >]
	Martial, Joseph [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
	Wyns, Lode [Vrije Universiteit Brussel > Vlaams Interuniversitair Instituut voor Biotechnologie > > >]
	Jaenicke, Rainer [Universität Regensburg > Institut für Biophysik und physikalische Biochemie > > >]
	Wierenga, Rik K. [European Molecular Biology Laboratory > > > >]
Publication date :	1999
Journal title :	Proteins
Publisher :	Wiley Liss, Inc.
Volume :	37
Issue/season :	3
Pages :	441-53
ISSN :	0887-3585
e-ISSN :	1097-0134
City :	New York
Country :	NY
Keywords :	[en] Amino Acid Sequence ; Crystallography, X-Ray ; Heating ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Structure, Secondary ; Sequence Alignment ; Thermotoga maritima/chemistry ; Triose-Phosphate Isomerase/chemistry
Abstract :	[en] The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM). The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its 3D-structure. It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles. Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs. A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process.
Permalink :	http://hdl.handle.net/2268/19823
DOI :	10.1002/(SICI)1097-0134(19991115)37:3<441::AID-PROT11>3.0.CO;2-7 [pii]
Other URL :	http://www3.interscience.wiley.com/journal/68502076/abstract?CRETRY=1&SRETRY=0
Mentions required by the publisher for OA :	1999/12/11

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