1ah2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "1ah2" [edit=sysop:move=sysop]
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ah2.png|left|200px]]


<!--
==SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES==
The line below this paragraph, containing "STRUCTURE_1ah2", creates the "Structure Box" on the page.
<StructureSection load='1ah2' size='340' side='right'caption='[[1ah2]]' 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'>[[1ah2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_alcalophilus Alkalihalobacillus alcalophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AH2 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">Solution NMR</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ah2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ah2 OCA], [https://pdbe.org/1ah2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ah2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ah2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ah2 ProSAT]</span></td></tr>
{{STRUCTURE_1ah2|  PDB=1ah2  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELYA_ALKAL ELYA_ALKAL]
== 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/ah/1ah2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ah2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Research on high-alkaline proteases, such as serine protease PB92, has been largely inspired by their industrial application as protein-degrading components of washing powders. Serine protease PB92 is a member of the subtilase family of enzymes, which has been extensively studied. These studies have included exhaustive protein engineering investigations and X-ray crystallography, in order to provide insight into the mechanism and specificity of enzyme catalysis. Distortions have been observed in the substrate-binding region of subtilisin crystal structures, due to crystal contacts. In addition, the structural variability in the substrate-binding region of subtilisins is often attributed to flexibility. It was hoped that the solution structure of this enzyme would provide further details about the conformation of this key region and give new insights into the functional properties of these enzymes. RESULTS: The three-dimensional solution structure of the 269-residue (27 kDa) serine protease PB92 has been determined using distance and dihedral angle constraints derived from triple-resonance NMR data. The solution structure is represented by a family of 18 conformers which overlay onto the average structure with backbone and all-heavy-atom root mean square deviations (for the main body of the molecule) of 0.88 and 1.21 A, respectively. The family of structures contains a number of regions of relatively high conformational heterogeneity, including various segments that are involved in the formation of the substrate-binding site. The presence of flexibility within these segments has been established from NMR relaxation parameters and measurements of amide proton exchange rates. CONCLUSIONS: The solution structure of the serine protease PB92 presents a well defined global fold which is rigid with the exception of a restricted number of sites. Among the limited number of residues involved in significant internal mobility are those of two pockets, termed S1 and S4, within the substrate-binding site. The presence of flexibility within the binding site supports the proposed induced fit mechanism of substrate binding.


===SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES===
The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site.,Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R Structure. 1997 Apr 15;5(4):521-32. PMID:9115441<ref>PMID:9115441</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_9115441}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1ah2" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 9115441 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_9115441}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Alkalihalobacillus alcalophilus]]
[[1ah2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_alcalophilus Bacillus alcalophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH2 OCA].
[[Category: Large Structures]]
 
[[Category: Boelens R]]
==Reference==
[[Category: Karimi-Nejad Y]]
<ref group="xtra">PMID:009115441</ref><ref group="xtra">PMID:017154716</ref><references group="xtra"/>
[[Category: Mariani M]]
[[Category: Bacillus alcalophilus]]
[[Category: Martin JR]]
[[Category: Boelens, R.]]
[[Category: Mulder F]]
[[Category: Karimi-Nejad, Y.]]
[[Category: Schipper D]]
[[Category: Mariani, M.]]
[[Category: Zwan JVD]]
[[Category: Martin, J R.]]
[[Category: Mulder, F.]]
[[Category: Schipper, D.]]
[[Category: Zwan, J V.D.]]
[[Category: Application in washing powder]]
[[Category: Industrial enzyme]]
[[Category: Serine protease]]
[[Category: Subtilase]]

Latest revision as of 11:13, 22 May 2024

SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURESSERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES

Structural highlights

1ah2 is a 1 chain structure with sequence from Alkalihalobacillus alcalophilus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ELYA_ALKAL

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Research on high-alkaline proteases, such as serine protease PB92, has been largely inspired by their industrial application as protein-degrading components of washing powders. Serine protease PB92 is a member of the subtilase family of enzymes, which has been extensively studied. These studies have included exhaustive protein engineering investigations and X-ray crystallography, in order to provide insight into the mechanism and specificity of enzyme catalysis. Distortions have been observed in the substrate-binding region of subtilisin crystal structures, due to crystal contacts. In addition, the structural variability in the substrate-binding region of subtilisins is often attributed to flexibility. It was hoped that the solution structure of this enzyme would provide further details about the conformation of this key region and give new insights into the functional properties of these enzymes. RESULTS: The three-dimensional solution structure of the 269-residue (27 kDa) serine protease PB92 has been determined using distance and dihedral angle constraints derived from triple-resonance NMR data. The solution structure is represented by a family of 18 conformers which overlay onto the average structure with backbone and all-heavy-atom root mean square deviations (for the main body of the molecule) of 0.88 and 1.21 A, respectively. The family of structures contains a number of regions of relatively high conformational heterogeneity, including various segments that are involved in the formation of the substrate-binding site. The presence of flexibility within these segments has been established from NMR relaxation parameters and measurements of amide proton exchange rates. CONCLUSIONS: The solution structure of the serine protease PB92 presents a well defined global fold which is rigid with the exception of a restricted number of sites. Among the limited number of residues involved in significant internal mobility are those of two pockets, termed S1 and S4, within the substrate-binding site. The presence of flexibility within the binding site supports the proposed induced fit mechanism of substrate binding.

The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site.,Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R Structure. 1997 Apr 15;5(4):521-32. PMID:9115441[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R. The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site. Structure. 1997 Apr 15;5(4):521-32. PMID:9115441
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA