1f34: Difference between revisions

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New page: left|200px<br /><applet load="1f34" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f34, resolution 2.45Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1f34.gif|left|200px]]<br /><applet load="1f34" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f34, resolution 2.45&Aring;" />
'''CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN==
The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris, suum and of the complex between PI-3 and porcine pepsin at 1. 75 A and, 2.45 A resolution, respectively, have revealed the mechanism of aspartic, protease inhibition by this unique inhibitor. PI-3 has a new fold, consisting of two domains, each comprising an antiparallel beta-sheet, flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal, beta-strand of PI-3 pairs with one strand of the 'active site flap', (residues 70-82) of pepsin, thus forming an eight-stranded beta-sheet that, spans the two proteins. PI-3 has a novel mode of inhibition, using its, N-terminal residues to occupy and therefore block the first three binding, pockets in pepsin for substrate residues C-terminal to the scissile bond, (S1'-S3'). The molecular structure of the pepsin-PI-3 complex suggests new, avenues for the rational design of proteinaceous aspartic proteinase, inhibitors.
<StructureSection load='1f34' size='340' side='right'caption='[[1f34]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F34 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=1f34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f34 OCA], [https://pdbe.org/1f34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f34 RCSB], [https://www.ebi.ac.uk/pdbsum/1f34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f34 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
== 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/f3/1f34_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=1f34 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F34 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA].
*[[Pepsin|Pepsin]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3., Ng KK, Petersen JF, Cherney MM, Garen C, Zalatoris JJ, Rao-Naik C, Dunn BM, Martzen MR, Peanasky RJ, James MN, Nat Struct Biol. 2000 Aug;7(8):653-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10932249 10932249]
[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Pepsin A]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Cherney, M.M.]]
[[Category: Cherney MM]]
[[Category: Garen, C.]]
[[Category: Garen C]]
[[Category: James, M.N.]]
[[Category: James MN]]
[[Category: Ng, K.K.]]
[[Category: Ng KK]]
[[Category: Petersen, J.F.]]
[[Category: Petersen JF]]
[[Category: MPD]]
[[Category: proteinase-inhibitor complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:34:02 2007''

Latest revision as of 13:09, 20 March 2024

CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSINCRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN

Structural highlights

1f34 is a 2 chain structure with sequence from Ascaris suum and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.45Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PEPA_PIG Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.

Evolutionary Conservation

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

See Also

1f34, resolution 2.45Å

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