1cer: Difference between revisions

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[[Image:1cer.gif|left|200px]]
[[Image:1cer.gif|left|200px]]


{{Structure
<!--
|PDB= 1cer |SIZE=350|CAPTION= <scene name='initialview01'>1cer</scene>, resolution 2.5&Aring;
The line below this paragraph, containing "STRUCTURE_1cer", 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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span>
or leave the SCENE parameter empty for the default display.
|GENE= THERMUS AQUATICUS GAPDH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus])
-->
|DOMAIN=
{{STRUCTURE_1cer| PDB=1cer  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cer OCA], [http://www.ebi.ac.uk/pdbsum/1cer PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cer RCSB]</span>
}}


'''DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION'''
'''DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION'''
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==Reference==
==Reference==
Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution., Tanner JJ, Hecht RM, Krause KL, Biochemistry. 1996 Feb 27;35(8):2597-609. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8611563 8611563]
Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution., Tanner JJ, Hecht RM, Krause KL, Biochemistry. 1996 Feb 27;35(8):2597-609. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8611563 8611563]
[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: Krause, K L.]]
[[Category: Krause, K L.]]
[[Category: Tanner, J J.]]
[[Category: Tanner, J J.]]
[[Category: glycolysis]]
[[Category: Glycolysis]]
[[Category: nad]]
[[Category: Nad]]
[[Category: oxidoreductase]]
[[Category: Oxidoreductase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:14 2008''

Revision as of 12:39, 2 May 2008

File:1cer.gif

Template:STRUCTURE 1cer

DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION


OverviewOverview

The crystal structure of holo D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the extreme thermophile Thermus aquaticus has been solved at 2.5 Angstroms resolution. To study the determinants of thermostability, we compare our structure to four other GAPDHs. Salt links, hydrogen bonds, buried surface area, packing density, surface to volume ratio, and stabilization of alpha-helices and beta-turns are analyzed. We find a strong correlation between thermostability and the number of hydrogen bonds between charged side chains and neutral partners. These charged-neutral hydrogen bonds provide electrostatic stabilization without the heavy desolvation penalty of salt links. The stability of thermophilic GAPDHs is also correlated with the number of intrasubunit salt links and total hydrogen bonds. Charged residues, therefore, play a dual role in stabilization by participating not only in salt links but also in hydrogen bonds with a neutral partner. Hydrophobic effects allow for discrimination between thermophiles and psychrophiles, but not within the GAPDH thermophiles. There is, however, an association between thermostability and decreasing enzyme surface to volume ratio. Finally, we describe several interactions present in both our GAPDH and a hyperthermophilic GAPDH that are absent in the less thermostable GAPDHs. These include a four-residue salt link network, a hydrogen bond near the active site, an intersubunit salt link, and several buried Ile residues.

About this StructureAbout this Structure

1CER is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.

ReferenceReference

Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution., Tanner JJ, Hecht RM, Krause KL, Biochemistry. 1996 Feb 27;35(8):2597-609. PMID:8611563 Page seeded by OCA on Fri May 2 12:39:08 2008

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