1wmm: Difference between revisions

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<StructureSection load='1wmm' size='340' side='right'caption='[[1wmm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1wmm' size='340' side='right'caption='[[1wmm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wmm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WMM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WMM FirstGlance]. <br>
</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=1wmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmm OCA], [http://pdbe.org/1wmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wmm RCSB], [http://www.ebi.ac.uk/pdbsum/1wmm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wmm ProSAT], [http://www.topsan.org/Proteins/RSGI/1wmm TOPSAN]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1wmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmm OCA], [https://pdbe.org/1wmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wmm RCSB], [https://www.ebi.ac.uk/pdbsum/1wmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wmm ProSAT], [https://www.topsan.org/Proteins/RSGI/1wmm TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y1033_PYRHO Y1033_PYRHO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1wmm ConSurf].
</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=1wmm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein crystallization is still a major bottleneck in structural biology. As the current methodology of protein crystallization is a type of screening, it is usually difficult to crystallize important target proteins. It was thought that hetero-epitaxic growth from the surface of a mineral crystal acting as a nucleant would be an effective enhancer of protein crystallization. However, in spite of almost two decades of effort, a generally applicable hetero-epitaxic nucleant for protein crystallization has yet to be found. Here we introduce the first candidate for a universal hetero-epitaxic nucleant, microporous zeolite: a synthetic aluminosilicate crystalline polymer with regular micropores. It promotes a form-selective crystal nucleation of proteins and acts as a crystallization catalyst. The most successful zeolite nucleant was molecular sieve type 5A with a pore size of 5 A and with bound Ca2+ ions. The zeolite-mediated crystallization improved the crystal quality in five out of six proteins tested. It provided new crystal forms with better resolution in two cases, larger crystals in one case, and zeolite-dependent crystal formations in two cases. The hetero-epitaxic growth of the zeolite-mediated crystals was confirmed by a crystal-packing analysis which revealed a layer-like structure in the crystal lattice.
Nucleant-mediated protein crystallization with the application of microporous synthetic zeolites.,Sugahara M, Asada Y, Morikawa Y, Kageyama Y, Kunishima N Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):686-95. Epub 2008, May 14. PMID:18560157<ref>PMID:18560157</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1wmm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrococcus shinkaii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kunishima, N]]
[[Category: Structural genomic]]
[[Category: Sugahara, M]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
[[Category: Rsgi]]
[[Category: Kunishima N]]
[[Category: Unknown function]]
[[Category: Sugahara M]]

Latest revision as of 16:32, 13 March 2024

Crystal structure of PH1033 from Pyrococcus horikoshii Ot3Crystal structure of PH1033 from Pyrococcus horikoshii Ot3

Structural highlights

1wmm is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

Y1033_PYRHO

Evolutionary Conservation

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

1wmm, resolution 2.20Å

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OCA
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