|
|
| Line 1: |
Line 1: |
| [[Image:1ba0.gif|left|200px]] | | {{Seed}} |
| | [[Image:1ba0.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1ba0| PDB=1ba0 | SCENE= }} | | {{STRUCTURE_1ba0| PDB=1ba0 | SCENE= }} |
|
| |
|
| '''HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE 3'''
| | ===HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE 3=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| We have assessed the ability of the epsilon-amino group of a non-native lysine chain to substitute for a monovalent cation in an enzyme active site. In the bovine Hsc70 ATPase fragment, mutation of cysteine 17 or aspartic acid 206 to lysine potentially allows the replacement of an active site potassium ion with the epsilon-amino nitrogen. We examined the ATP hydrolysis kinetics and crystal structures of isolated mutant ATPase domains. The introduced epsilon-amino nitrogen in the C17K mutant occupies a significantly different position than the potassium ion. The introduced epsilon-amino nitrogen in the D206K mutant occupies a position indistinguishable from that of the potassium in the wild-type structure. Each mutant retains <5% ATPase activity when compared to the wild type under physiological conditions (potassium buffer) although substrate binding is tighter, probably as a consequence of slower release. It is possible to construct a very good structural mimic of bound cation which suffices for substrate binding but not for catalytic activity.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9585559}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9585559 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_9585559}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| [[Category: Heat shock]] | | [[Category: Heat shock]] |
| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:15:44 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:40:23 2008'' |
