3kl9: Difference between revisions

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==Crystal structure of PepA from Streptococcus pneumoniae==
==Crystal structure of PepA from Streptococcus pneumoniae==
<StructureSection load='3kl9' size='340' side='right' caption='[[3kl9]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3kl9' size='340' side='right'caption='[[3kl9]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3kl9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KL9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3kl9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KL9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 STRR6])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_aminopeptidase Glutamyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.7 3.4.11.7] </span></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=3kl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl9 OCA], [https://pdbe.org/3kl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kl9 RCSB], [https://www.ebi.ac.uk/pdbsum/3kl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl9 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl9 OCA], [http://pdbe.org/3kl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kl9 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8DNJ7_STRR6 Q8DNJ7_STRR6]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/3kl9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/3kl9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</div>
</div>
<div class="pdbe-citations 3kl9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3kl9" style="background-color:#fffaf0;"></div>
==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutamyl aminopeptidase]]
[[Category: Large Structures]]
[[Category: Strr6]]
[[Category: Streptococcus pneumoniae R6]]
[[Category: Kim, D]]
[[Category: Kim D]]
[[Category: Kim, K K]]
[[Category: Kim KK]]
[[Category: Lee, S]]
[[Category: Lee S]]
[[Category: Aminopeptidase]]
[[Category: Hydrolase]]
[[Category: Metallopeptidase m42]]
[[Category: Pepa]]
[[Category: Substrate specificity]]
[[Category: Tetrahedral aminopeptidase]]

Latest revision as of 19:13, 1 November 2023

Crystal structure of PepA from Streptococcus pneumoniaeCrystal structure of PepA from Streptococcus pneumoniae

Structural highlights

3kl9 is a 12 chain structure with sequence from Streptococcus pneumoniae R6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8DNJ7_STRR6

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

Regulated cytosolic proteolysis is one of the key cellular processes ensuring proper functioning of a cell. M42 family proteases show a broad spectrum of substrate specificities, but the structural basis for such diversity of the substrate specificities is lagging behind biochemical data. Here we report the crystal structure of PepA from Streptococcus pneumoniae, a glutamyl aminopeptidase belonging to M42 family (SpPepA). We found that Arg-257 in the substrate binding pocket is strategically positioned so that Arg-257 can make electrostatic interactions with the acidic residue of a substrate at its N-terminus. Structural comparison of the substrate binding pocket of the M42 family proteases, along with the structure-based multiple sequence alignment, argues that the appropriate electrostatic interactions contribute to the selective substrate specificity of SpPepA.

Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease.,Kim D, San BH, Moh SH, Park H, Kim DY, Lee S, Kim KK Biochem Biophys Res Commun. 2010 Jan 1;391(1):431-6. Epub 2009 Nov 13. PMID:19914209[1]

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

See Also

References

  1. Kim D, San BH, Moh SH, Park H, Kim DY, Lee S, Kim KK. Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease. Biochem Biophys Res Commun. 2010 Jan 1;391(1):431-6. Epub 2009 Nov 13. PMID:19914209 doi:10.1016/j.bbrc.2009.11.075

3kl9, resolution 2.70Å

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OCA