|
|
| Line 1: |
Line 1: |
| [[Image:2iyr.gif|left|200px]] | | {{Seed}} |
| | [[Image:2iyr.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2iyr| PDB=2iyr | SCENE= }} | | {{STRUCTURE_2iyr| PDB=2iyr | SCENE= }} |
|
| |
|
| '''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE'''
| | ===SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate. | | The line below this paragraph, {{ABSTRACT_PUBMED_17020768}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17020768 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17020768}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 39: |
Line 43: |
| [[Category: Shikimate pathway]] | | [[Category: Shikimate pathway]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:05:27 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:01:36 2008'' |