1s2n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:48, 6 November 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1s2n.gif|left|200px]]
 
-
<!--
+
==Crystal structure of a cold adapted subtilisin-like serine proteinase==
-
The line below this paragraph, containing "STRUCTURE_1s2n", creates the "Structure Box" on the page.
+
<StructureSection load='1s2n' size='340' side='right'caption='[[1s2n]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1s2n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_sp._PA-44 Vibrio sp. PA-44]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S2N FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.44&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</scene></td></tr>
-
{{STRUCTURE_1s2n| PDB=1s2n | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2n OCA], [https://pdbe.org/1s2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s2n RCSB], [https://www.ebi.ac.uk/pdbsum/1s2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s2n ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q8GB52_9VIBR Q8GB52_9VIBR]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s2/1s2n_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s2n ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The crystal structure of a subtilisin-like serine proteinase from the psychrotrophic marine bacterium, Vibrio sp. PA-44, was solved by means of molecular replacement and refined at 1.84 A. This is the first structure of a cold-adapted subtilase to be determined and its elucidation facilitates examination of the molecular principles underlying temperature adaptation in enzymes. The cold-adapted Vibrio proteinase was compared with known three-dimensional structures of homologous enzymes of meso- and thermophilic origin, proteinase K and thermitase, to which it has high structural resemblance. The main structural features emerging as plausible determinants of temperature adaptation in the enzymes compared involve the character of their exposed and buried surfaces, which may be related to temperature-dependent variation in the physical properties of water. Thus, the hydrophobic effect is found to play a significant role in the structural stability of the meso- and thermophile enzymes, whereas the cold-adapted enzyme has more of its apolar surface exposed. In addition, the cold-adapted Vibrio proteinase is distinguished from the more stable enzymes by its strong anionic character arising from the high occurrence of uncompensated negatively charged residues at its surface. Interestingly, both the cold-adapted and thermophile proteinases differ from the mesophile enzyme in having more extensive hydrogen- and ion pair interactions in their structures; this supports suggestions of a dual role of electrostatic interactions in the adaptation of enzymes to both high and low temperatures. The Vibrio proteinase has three calcium ions associated with its structure, one of which is in a calcium-binding site not described in other subtilases.
-
'''Crystal strucure of a cold adapted subtilisin-like serine proteinase'''
+
Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation.,Arnorsdottir J, Kristjansson MM, Ficner R FEBS J. 2005 Feb;272(3):832-45. PMID:15670163<ref>PMID:15670163</ref>
-
 
+
-
 
+
-
==Overview==
+
-
The crystal structure of a subtilisin-like serine proteinase from the psychrotrophic marine bacterium, Vibrio sp. PA-44, was solved by means of molecular replacement and refined at 1.84 A. This is the first structure of a cold-adapted subtilase to be determined and its elucidation facilitates examination of the molecular principles underlying temperature adaptation in enzymes. The cold-adapted Vibrio proteinase was compared with known three-dimensional structures of homologous enzymes of meso- and thermophilic origin, proteinase K and thermitase, to which it has high structural resemblance. The main structural features emerging as plausible determinants of temperature adaptation in the enzymes compared involve the character of their exposed and buried surfaces, which may be related to temperature-dependent variation in the physical properties of water. Thus, the hydrophobic effect is found to play a significant role in the structural stability of the meso- and thermophile enzymes, whereas the cold-adapted enzyme has more of its apolar surface exposed. In addition, the cold-adapted Vibrio proteinase is distinguished from the more stable enzymes by its strong anionic character arising from the high occurrence of uncompensated negatively charged residues at its surface. Interestingly, both the cold-adapted and thermophile proteinases differ from the mesophile enzyme in having more extensive hydrogen- and ion pair interactions in their structures; this supports suggestions of a dual role of electrostatic interactions in the adaptation of enzymes to both high and low temperatures. The Vibrio proteinase has three calcium ions associated with its structure, one of which is in a calcium-binding site not described in other subtilases.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1S2N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2N OCA].
+
</div>
 +
<div class="pdbe-citations 1s2n" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation., Arnorsdottir J, Kristjansson MM, Ficner R, FEBS J. 2005 Feb;272(3):832-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15670163 15670163]
+
*[[Proteinase 3D structures|Proteinase 3D structures]]
-
[[Category: Bacteria]]
+
== References ==
-
[[Category: Single protein]]
+
<references/>
-
[[Category: Arnorsdottir, J.]]
+
__TOC__
-
[[Category: Ficner, R.]]
+
</StructureSection>
-
[[Category: Kristjansson, M M.]]
+
[[Category: Large Structures]]
-
[[Category: Hydrolase]]
+
[[Category: Vibrio sp. PA-44]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:13:13 2008''
+
[[Category: Arnorsdottir J]]
 +
[[Category: Ficner R]]
 +
[[Category: Kristjansson MM]]

Current revision

Crystal structure of a cold adapted subtilisin-like serine proteinase

PDB ID 1s2n

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s2n"
Personal tools