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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=''>
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<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='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='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='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'>[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]</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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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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|Aminopeptidase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 11:35, 1 November 2017

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

Structural highlights

3kl9 is a 12 chain structure with sequence from Strr6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:pepA (STRR6)
Activity:Glutamyl aminopeptidase, with EC number 3.4.11.7
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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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