1ssg: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 4: Line 4:
|PDB= 1ssg |SIZE=350|CAPTION= <scene name='initialview01'>1ssg</scene>, resolution 2.90&Aring;
|PDB= 1ssg |SIZE=350|CAPTION= <scene name='initialview01'>1ssg</scene>, resolution 2.90&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY= [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]  
|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>
|GENE= TPI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
|GENE= TPI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
|DOMAIN=
|RELATEDENTRY=[[1spq|1SPQ]], [[1sq7|1SQ7]], [[1ssd|1SSD]], [[1su5|1SU5]], [[1sw0|1SW0]], [[1sw3|1SW3]], [[1sw7|1SW7]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ssg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssg OCA], [http://www.ebi.ac.uk/pdbsum/1ssg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ssg RCSB]</span>
}}
}}


Line 30: Line 33:
[[Category: Sun, J.]]
[[Category: Sun, J.]]
[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
[[Category: GOL]]
[[Category: PGA]]
[[Category: SO4]]
[[Category: archae]]
[[Category: archae]]
[[Category: evolution]]
[[Category: evolution]]
Line 39: Line 39:
[[Category: tim]]
[[Category: tim]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:09:04 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:21 2008''

Revision as of 23:46, 30 March 2008

File:1ssg.gif


PDB ID 1ssg

Drag the structure with the mouse to rotate
, resolution 2.90Å
Ligands: , ,
Gene: TPI1 (Gallus gallus)
Activity: Triose-phosphate isomerase, with EC number 5.3.1.1
Related: 1SPQ, 1SQ7, 1SSD, 1SU5, 1SW0, 1SW3, 1SW7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase


OverviewOverview

The conformational switch from open to closed of the flexible loop 6 of triosephosphate isomerase (TIM) is essential for the catalytic properties of TIM. Using a directed evolution approach, active variants of chicken TIM with a mutated C-terminal hinge tripeptide of loop 6 have been generated (Sun,J. and Sampson,N.S., Biochemistry, 1999, 38, 11474-11481). In chicken TIM, the wild-type C-terminal hinge tripeptide is KTA. Detailed enzymological characterization of six variants showed that some of these (LWA, NPN, YSL, KTK) have decreased catalytic efficiency, whereas others (KVA, NSS) are essentially identical with wild-type. The structural characterization of these six variants is reported. No significant structural differences compared with the wild-type are found for KVA, NSS and LWA, but substantial structural adaptations are seen for NPN, YSL and KTK. These structural differences can be understood from the buried position of the alanine side chain in the C-hinge position 3 in the open conformation of wild-type loop 6. Replacement of this alanine with a bulky side chain causes the closed conformation to be favored, which correlates with the decreased catalytic efficiency of these variants. The structural context of loop 6 and loop 7 and their sequence conservation in 133 wild-type sequences is also discussed.

About this StructureAbout this Structure

1SSG is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase., Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK, Protein Eng Des Sel. 2004 Apr;17(4):375-82. Epub 2004 May 27. PMID:15166315

Page seeded by OCA on Sun Mar 30 23:46:21 2008

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

OCA