We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2bjd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bjd.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bjd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bjd| PDB=2bjd | SCENE= }}
{{STRUCTURE_2bjd| PDB=2bjd | SCENE= }}
-
'''SULFOLOBUS SOLFATARICUS ACYLPHOSPHATASE. TRICLINIC SPACE GROUP'''
+
===SULFOLOBUS SOLFATARICUS ACYLPHOSPHATASE. TRICLINIC SPACE GROUP===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16287076}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16287076 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16287076}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Hyperthermophile]]
[[Category: Hyperthermophile]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:22:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:15:34 2008''

Revision as of 03:15, 29 July 2008

Image:2bjd.png

Template:STRUCTURE 2bjd

SULFOLOBUS SOLFATARICUS ACYLPHOSPHATASE. TRICLINIC SPACE GROUP

Template:ABSTRACT PUBMED 16287076

About this Structure

2BJD is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic 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

Page seeded by OCA on Tue Jul 29 06:15:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bjd"
Personal tools