From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1wm6.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1wm6.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1wm6| PDB=1wm6 | SCENE= }} | | {{STRUCTURE_1wm6| PDB=1wm6 | SCENE= }} |
| | | | |
| - | '''Crystal structure of TT0310 protein from Thermus thermophilus HB8'''
| + | ===Crystal structure of TT0310 protein from Thermus thermophilus HB8=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Hot dog fold proteins sharing the characteristic "hot dog" fold are known to involve certain coenzyme A binding enzymes with various oligomeric states. In order to elucidate the oligomerization-function relationship of the hot dog fold proteins, crystal structures of the phenylacetate degradation protein PaaI from Thermus thermophilus HB8 (TtPaaI), a tetrameric acyl-CoA thioesterase with the hot dog fold, have been determined and compared with those of other family members. In the liganded crystal forms with coenzyme A derivatives, only two of four intersubunit catalytic pockets of the TtPaaI tetramer are occupied by the ligands. A detailed structural comparison between several liganded and unliganded forms reveals that a subtle rigid-body rearrangement of subunits within 2 degrees upon binding of the first two ligand molecules can induce a strict negative cooperativity to prevent further binding at the remaining two pockets, indicating that the so-called "half-of-the-sites reactivity" of oligomeric enzymes is visualized for the first time. Considering kinetic and mutational analyses together, a possible reaction mechanism of TtPaaI is proposed; one tetramer binds only two acyl-CoA molecules with a novel asymmetric induced-fit mechanism and carries out the hydrolysis according to a base-catalyzed reaction through activation of a water molecule by Asp48. From a structural comparison with other family members, it is concluded that a subgroup of the hot dog fold protein family, referred to as "asymmetric hot dog thioesterases" including medium chain acyl-CoA thioesterase II from Escherichia coli and human thioesterase III, might share the same oligomerization mode and the asymmetric induced-fit mechanism as observed in TtPaaI.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16061252}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16061252 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16061252}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| | [[Category: Thioesterase]] | | [[Category: Thioesterase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:51:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:16:02 2008'' |
Revision as of 01:16, 29 July 2008
Template:STRUCTURE 1wm6
Crystal structure of TT0310 protein from Thermus thermophilus HB8
Template:ABSTRACT PUBMED 16061252
About this Structure
1WM6 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
A novel induced-fit reaction mechanism of asymmetric hot dog thioesterase PAAI., Kunishima N, Asada Y, Sugahara M, Ishijima J, Nodake Y, Sugahara M, Miyano M, Kuramitsu S, Yokoyama S, Sugahara M, J Mol Biol. 2005 Sep 9;352(1):212-28. PMID:16061252
Page seeded by OCA on Tue Jul 29 04:16:02 2008
