1b9b: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1b9b.jpg|left|200px]]
[[Image:1b9b.jpg|left|200px]]


{{Structure
<!--
|PDB= 1b9b |SIZE=350|CAPTION= <scene name='initialview01'>1b9b</scene>, resolution 2.85&Aring;
The line below this paragraph, containing "STRUCTURE_1b9b", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1b9b| PDB=1b9b  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9b OCA], [http://www.ebi.ac.uk/pdbsum/1b9b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b9b RCSB]</span>
}}


'''TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA'''
'''TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA'''
Line 28: Line 25:
[[Category: Maes, D.]]
[[Category: Maes, D.]]
[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
[[Category: isomerase]]
[[Category: Isomerase]]
[[Category: thermophilic]]
[[Category: Thermophilic]]
[[Category: thermotoga maritima]]
[[Category: Thermotoga maritima]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:14:09 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:56:15 2008''

Revision as of 11:14, 2 May 2008

File:1b9b.jpg

Template:STRUCTURE 1b9b

TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA


OverviewOverview

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.

About this StructureAbout this Structure

1B9B is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures., Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK, Proteins. 1999 Nov 15;37(3):441-53. PMID:10591103 Page seeded by OCA on Fri May 2 11:14:09 2008

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

OCA