1ba0
From Proteopedia
(New page: 200px<br /><applet load="1ba0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ba0, resolution 1.9Å" /> '''HEAT-SHOCK COGNATE 70...) |
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| - | [[Image:1ba0.gif|left|200px]]<br /><applet load="1ba0" size=" | + | [[Image:1ba0.gif|left|200px]]<br /><applet load="1ba0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ba0, resolution 1.9Å" /> | caption="1ba0, resolution 1.9Å" /> | ||
'''HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE 3'''<br /> | '''HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE 3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have assessed the ability of the epsilon-amino group of a non-native | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, PO4, NA, CL and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http:// | + | 1BA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BA0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Mckay, D | + | [[Category: Mckay, D B.]] |
| - | [[Category: Wilbanks, S | + | [[Category: Wilbanks, S M.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:06 2008'' |
Revision as of 09:53, 21 February 2008
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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.
About this Structure
1BA0 is a Single protein structure of sequence from Bos taurus with , , , and as ligands. Active as Adenosinetriphosphatase, with EC number 3.6.1.3 Full crystallographic information is available from OCA.
Reference
Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70., Wilbanks SM, McKay DB, Biochemistry. 1998 May 19;37(20):7456-62. PMID:9585559
Page seeded by OCA on Thu Feb 21 11:53:06 2008
Categories: Adenosinetriphosphatase | Bos taurus | Single protein | Mckay, D B. | Wilbanks, S M. | ADP | CL | MG | NA | PO4 | Acting on acid anhydrides | Atp-binding | Heat shock | Hydrolase
