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1fiz

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(New page: 200px<br /><applet load="1fiz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fiz, resolution 2.9&Aring;" /> '''THREE DIMENSIONAL STR...)
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[[Image:1fiz.gif|left|200px]]<br /><applet load="1fiz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fiz, resolution 2.9&Aring;" />
 
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'''THREE DIMENSIONAL STRUCTURE OF BETA-ACROSIN FROM BOAR SPERMATOZOA'''<br />
 
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==Overview==
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==THREE DIMENSIONAL STRUCTURE OF BETA-ACROSIN FROM BOAR SPERMATOZOA==
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BACKGROUND: Proacrosin is a serine protease found specifically within the, acrosomal vesicle of all mammalian spermatozoa. During fertilization, proacrosin autoactivates to form beta-acrosin, in which there is a "light", chain cross-linked to a "heavy" chain by two disulphide bonds., beta-acrosin is thought to be multifunctional with roles in acrosomal, exocytosis, as a receptor for zona pellucida proteins, and as a protease, to facilitate penetration of spermatozoa into the egg. RESULTS: The, crystal structures of both ram and boar beta-acrosins have been solved in, complex with p-aminobenzamidine to 2.1 A and 2.9 A resolution, respectively. Both enzymes comprise a heavy chain with structural homology, to trypsin, and a light chain covalently associated in a similar manner to, blood coagulation enzymes. In crystals of boar beta-acrosin, the carboxyl, terminus of the heavy chain is inserted into the active site of the, neighboring molecule. In both enzyme structures, there are distinctive, positively charged surface "patches" close to the active site, which, associate with carbohydrate from adjacent molecules and also bind sulfate, ions. CONCLUSIONS: From the three-dimensional structure of beta-acrosin, two separate effector sites are evident. First, proteolytic activity, believed to be important at various stages during fertilization, arises, from the trypsin-like active site. Activity of this site may be, autoregulated through intermolecular associations. Second, positively, charged regions on the surface adjacent to the active site may act as, receptors for binding zona pellucida glycoproteins. The spatial proximity, of these two effector sites suggests there may be synergy between them.
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<StructureSection load='1fiz' size='340' side='right'caption='[[1fiz]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fiz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FIZ FirstGlance]. <br>
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1FIZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 and PBZ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FIZ OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PBZ:P-AMINO+BENZAMIDINE'>PBZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fiz OCA], [https://pdbe.org/1fiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fiz RCSB], [https://www.ebi.ac.uk/pdbsum/1fiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fiz ProSAT]</span></td></tr>
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Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin., Tranter R, Read JA, Jones R, Brady RL, Structure. 2000 Nov 15;8(11):1179-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080640 11080640]
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</table>
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[[Category: Protein complex]]
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== Function ==
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[https://www.uniprot.org/uniprot/ACRO_PIG ACRO_PIG] Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/1fiz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fiz ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Brady, R.L.]]
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[[Category: Brady RL]]
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[[Category: Jones, R.]]
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[[Category: Jones R]]
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[[Category: Read, J.A.]]
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[[Category: Read JA]]
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[[Category: Tranter, R.]]
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[[Category: Tranter R]]
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[[Category: PBZ]]
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[[Category: SO4]]
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[[Category: anti-parallel beta-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:57:32 2007''
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Current revision

THREE DIMENSIONAL STRUCTURE OF BETA-ACROSIN FROM BOAR SPERMATOZOA

PDB ID 1fiz

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