2oua
From Proteopedia
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| - | [[Image:2oua.gif|left|200px]] | + | [[Image:2oua.gif|left|200px]] |
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| - | '''Crystal Structure of Nocardiopsis Protease (NAPase)''' | + | {{Structure |
| + | |PDB= 2oua |SIZE=350|CAPTION= <scene name='initialview01'>2oua</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=2AB:4-(2-AMINOETHYL)BENZENESULFONIC+ACID'>2AB</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Nocardiopsis Protease (NAPase)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OUA is a [ | + | 2OUA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Nocardiopsis_alba Nocardiopsis alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUA OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior., Kelch BA, Eagen KP, Erciyas FP, Humphris EL, Thomason AR, Mitsuiki S, Agard DA, J Mol Biol. 2007 May 4;368(3):870-83. Epub 2007 Feb 22. PMID:[http:// | + | Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior., Kelch BA, Eagen KP, Erciyas FP, Humphris EL, Thomason AR, Mitsuiki S, Agard DA, J Mol Biol. 2007 May 4;368(3):870-83. Epub 2007 Feb 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17382344 17382344] |
[[Category: Nocardiopsis alba]] | [[Category: Nocardiopsis alba]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| - | [[Category: serine protease; kinetic stability; acid stability; | + | [[Category: serine protease; kinetic stability; acid stability; electrostatic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:04:32 2008'' |
Revision as of 16:04, 20 March 2008
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| , resolution 1.85Å | |||||||
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| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Nocardiopsis Protease (NAPase)
Overview
Kinetically stable proteins are unique in that their stability is determined solely by kinetic barriers rather than by thermodynamic equilibria. To better understand how kinetic stability promotes protein survival under extreme environmental conditions, we analyzed the unfolding behavior and determined the structure of Nocardiopsis alba Protease A (NAPase), an acid-resistant, kinetically stable protease, and compared these results with a neutrophilic homolog, alpha-lytic protease (alphaLP). Although NAPase and alphaLP have the same number of acid-titratable residues, kinetic studies revealed that the height of the unfolding free energy barrier for NAPase is less sensitive to acid than that of alphaLP, thereby accounting for NAPase's improved tolerance of low pH. A comparison of the alphaLP and NAPase structures identified multiple salt-bridges in the domain interface of alphaLP that were relocated to outer regions of NAPase, suggesting a novel mechanism of acid stability in which acid-sensitive electrostatic interactions are rearranged to similarly affect the energetics of both the native state and the unfolding transition state. An acid-stable variant of alphaLP in which a single interdomain salt-bridge is replaced with a corresponding intradomain NAPase salt-bridge shows a dramatic >15-fold increase in acid resistance, providing further evidence for this hypothesis. These observations also led to a general model of the unfolding transition state structure for alphaLP protease family members in which the two domains separate from each other while remaining relatively intact themselves. These results illustrate the remarkable utility of kinetic stability as an evolutionary tool for developing longevity over a broad range of harsh conditions.
About this Structure
2OUA is a Single protein structure of sequence from Nocardiopsis alba. Full crystallographic information is available from OCA.
Reference
Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior., Kelch BA, Eagen KP, Erciyas FP, Humphris EL, Thomason AR, Mitsuiki S, Agard DA, J Mol Biol. 2007 May 4;368(3):870-83. Epub 2007 Feb 22. PMID:17382344
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