1uh8: Difference between revisions
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==Crystal structure of rhizopuspepsin at pH 8.0== | |||
<StructureSection load='1uh8' size='340' side='right'caption='[[1uh8]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1uh8]] 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=1UH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UH8 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]] 2.3Å</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=1uh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uh8 OCA], [https://pdbe.org/1uh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uh8 RCSB], [https://www.ebi.ac.uk/pdbsum/1uh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uh8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CARP_RHICH CARP_RHICH] | |||
== 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/uh/1uh8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1uh8 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uh8" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Pepsin|Pepsin]] | *[[Pepsin|Pepsin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Rhizopus microsporus var. chinensis]] | [[Category: Rhizopus microsporus var. chinensis]] | ||
[[Category: Prasad | [[Category: Prasad BVLS]] | ||
[[Category: Suguna | [[Category: Suguna K]] | ||
Latest revision as of 03:33, 21 November 2024
Crystal structure of rhizopuspepsin at pH 8.0Crystal structure of rhizopuspepsin at pH 8.0
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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