1y9o

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{{STRUCTURE_1y9o| PDB=1y9o | SCENE= }}
{{STRUCTURE_1y9o| PDB=1y9o | SCENE= }}
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'''1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus'''
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===1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus===
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==Overview==
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The structure of AcP from the hyperthermophilic archaeon Sulfolobus solfataricus has been determined by (1)H-NMR spectroscopy and X-ray crystallography. Solution and crystal structures (1.27 A resolution, R-factor 13.7%) were obtained on the full-length protein and on an N-truncated form lacking the first 12 residues, respectively. The overall Sso AcP fold, starting at residue 13, displays the same betaalphabetabetaalphabeta topology previously described for other members of the AcP family from mesophilic sources. The unstructured N-terminal tail may be crucial for the unusual aggregation mechanism of Sso AcP previously reported. Sso AcP catalytic activity is reduced at room temperature but rises at its working temperature to values comparable to those displayed by its mesophilic counterparts at 25-37 degrees C. Such a reduced activity can result from protein rigidity and from the active site stiffening due the presence of a salt bridge between the C-terminal carboxylate and the active site arginine. Sso AcP is characterized by a melting temperature, Tm, of 100.8 degrees C and an unfolding free energy, DeltaG(U-F)H2O, at 28 degrees C and 81 degrees C of 48.7 and 20.6 kJ mol(-1), respectively. The kinetic and structural data indicate that mesophilic and hyperthermophilic AcP's display similar enzymatic activities and conformational stabilities at their working conditions. Structural analysis of the factor responsible for Sso AcP thermostability with respect to mesophilic AcP's revealed the importance of a ion pair network stabilizing particularly the beta-sheet and the loop connecting the fourth and fifth strands, together with increased density packing, loop shortening and a higher alpha-helical propensity.
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(as it appears on PubMed at http://www.pubmed.gov), where 16287076 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16287076}}
==About this Structure==
==About this Structure==
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1Y9O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9O OCA].
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1Y9O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9O OCA].
==Reference==
==Reference==
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus., Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P, Proteins. 2006 Jan 1;62(1):64-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16287076 16287076]
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus., Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P, Proteins. 2006 Jan 1;62(1):64-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16287076 16287076]
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Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation., Plakoutsi G, Taddei N, Stefani M, Chiti F, J Biol Chem. 2004 Apr 2;279(14):14111-9. Epub 2004 Jan 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14724277 14724277]
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Crystal structure of common type acylphosphatase from bovine testis., Thunnissen MM, Taddei N, Liguri G, Ramponi G, Nordlund P, Structure. 1997 Jan 15;5(1):69-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9016712 9016712]
[[Category: Acylphosphatase]]
[[Category: Acylphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Nmr]]
[[Category: Nmr]]
[[Category: Sso]]
[[Category: Sso]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:02:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:09:41 2008''

Revision as of 03:09, 29 July 2008

Image:1y9o.png

Template:STRUCTURE 1y9o

1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus

Template:ABSTRACT PUBMED 16287076

About this Structure

1Y9O is a Single protein structure of sequence from Sulfolobus solfataricus. Full experimental information is available from OCA.

Reference

Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus., Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P, Proteins. 2006 Jan 1;62(1):64-79. PMID:16287076

Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation., Plakoutsi G, Taddei N, Stefani M, Chiti F, J Biol Chem. 2004 Apr 2;279(14):14111-9. Epub 2004 Jan 14. PMID:14724277

Crystal structure of common type acylphosphatase from bovine testis., Thunnissen MM, Taddei N, Liguri G, Ramponi G, Nordlund P, Structure. 1997 Jan 15;5(1):69-79. PMID:9016712

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