1uh7

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[[Image:1uh7.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of rhizopuspepsin at pH 4.6==
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|PDB= 1uh7 |SIZE=350|CAPTION= <scene name='initialview01'>1uh7</scene>, resolution 2.1&Aring;
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<StructureSection load='1uh7' size='340' side='right'caption='[[1uh7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1uh7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizopus_microsporus_var._chinensis Rhizopus microsporus var. chinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UH7 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] </span>
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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]] 2.1&#8491;</td></tr>
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|GENE=
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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=1uh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uh7 OCA], [https://pdbe.org/1uh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uh7 RCSB], [https://www.ebi.ac.uk/pdbsum/1uh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uh7 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[2apr|2APR]], [[1uh8|1UH8]], [[1uh9|1UH9]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uh7 OCA], [http://www.ebi.ac.uk/pdbsum/1uh7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uh7 RCSB]</span>
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[https://www.uniprot.org/uniprot/CARP_RHICH CARP_RHICH]
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}}
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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/uh/1uh7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1uh7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range.
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'''Crystal structure of rhizopuspepsin at pH 4.6'''
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Effect of pH on the structure of rhizopuspepsin.,Prasad BV, Suguna K Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1755-61. Epub 2003, Sep 19. PMID:14501114<ref>PMID:14501114</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1uh7" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range.
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*[[Pepsin|Pepsin]]
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== References ==
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==About this Structure==
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<references/>
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1UH7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhizopus_microsporus_var._chinensis Rhizopus microsporus var. chinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UH7 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Effect of pH on the structure of rhizopuspepsin., Prasad BV, Suguna K, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1755-61. Epub 2003, Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14501114 14501114]
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[[Category: Hydrolase]]
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[[Category: Rhizopus microsporus var. chinensis]]
[[Category: Rhizopus microsporus var. chinensis]]
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[[Category: Single protein]]
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[[Category: Prasad BVLS]]
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[[Category: Prasad, B V.L S.]]
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[[Category: Suguna K]]
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[[Category: Suguna, K.]]
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[[Category: aspartic proteinase]]
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[[Category: pepsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:10:13 2008''
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Current revision

Crystal structure of rhizopuspepsin at pH 4.6

PDB ID 1uh7

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