From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1e6c.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1e6c.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1e6c| PDB=1e6c | SCENE= }} | | {{STRUCTURE_1e6c| PDB=1e6c | SCENE= }} |
| | | | |
| - | '''K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI'''
| + | ===K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Shikimate kinase, despite low sequence identity, has been shown to be structurally a member of the nucleoside monophosphate (NMP) kinase family, which includes adenylate kinase. In this paper we have explored the roles of residues in the P-loop of shikimate kinase, which forms the binding site for nucleotides and is one of the most conserved structural features in proteins. In common with many members of the P-loop family, shikimate kinase contains a cysteine residue 2 amino acids upstream of the essential lysine residue; the side chains of these residues are shown to form an ion pair. The C13S mutant of shikimate kinase was found to be enzymatically active, whereas the K15M mutant was inactive. However, the latter mutant had both increased thermostability and affinity for ATP when compared to the wild-type enzyme. The structure of the K15M mutant protein has been determined at 1.8 A, and shows that the organization of the P-loop and flanking regions is heavily disturbed. This indicates that, besides its role in catalysis, the P-loop lysine also has an important structural role. The structure of the K15M mutant also reveals that the formation of an additional arginine/aspartate ion pair is the most likely reason for its increased thermostability. From studies of ligand binding it appears that, like adenylate kinase, shikimate kinase binds substrates randomly and in a synergistic fashion, indicating that the two enzymes have similar catalytic mechanisms.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11369852}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11369852 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11369852}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Shikimate pathway]] | | [[Category: Shikimate pathway]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:43:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:13:32 2008'' |
Revision as of 21:13, 30 June 2008
Template:STRUCTURE 1e6c
K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI
Template:ABSTRACT PUBMED 11369852
About this Structure
1E6C is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
Reference
Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine., Krell T, Maclean J, Boam DJ, Cooper A, Resmini M, Brocklehurst K, Kelly SM, Price NC, Lapthorn AJ, Coggins JR, Protein Sci. 2001 Jun;10(6):1137-49. PMID:11369852
Page seeded by OCA on Tue Jul 1 00:13:32 2008
