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1crn

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(New page: 200px<br /><applet load="1crn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1crn, resolution 1.5&Aring;" /> '''WATER STRUCTURE OF A ...)
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[[Image:1crn.jpg|left|200px]]<br /><applet load="1crn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1crn, resolution 1.5&Aring;" />
 
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'''WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC RESOLUTION. PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF CRAMBIN'''<br />
 
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==Overview==
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==WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC RESOLUTION. PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF CRAMBIN==
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The water structure has been analyzed for a model of the protein crambin, refined against 0.945-A x-ray diffraction data. Crystals contain 32%, solvent by volume, and 77% of the solvent molecules have been, located-i.e., 2 ethanol molecules and 64 water molecules with 10-14, alternate positions. Many water oxygen atoms found form chains between, polar groups on the surface of the protein. However, a cluster of, pentagonal arrays made up of 16 water molecules sits at a hydrophobic, intermolecular cleft and forms a cap around the methyl group of, leucine-18. Several waters in the cluster are hydrogen-bonded directly to, the protein. Additional closed circular arrays, which include both protein, atoms and other water oxygen atoms, form next to the central cluster. This, water array stretches in the b lattice direction between groups of three, ionic side chains.
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<StructureSection load='1crn' size='340' side='right'caption='[[1crn]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1crn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRN FirstGlance]. <br>
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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]] 1.5&#8491;</td></tr>
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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=1crn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crn OCA], [https://pdbe.org/1crn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1crn RCSB], [https://www.ebi.ac.uk/pdbsum/1crn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1crn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
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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/cr/1crn_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=1crn 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 water structure has been analyzed for a model of the protein crambin refined against 0.945-A x-ray diffraction data. Crystals contain 32% solvent by volume, and 77% of the solvent molecules have been located-i.e., 2 ethanol molecules and 64 water molecules with 10-14 alternate positions. Many water oxygen atoms found form chains between polar groups on the surface of the protein. However, a cluster of pentagonal arrays made up of 16 water molecules sits at a hydrophobic, intermolecular cleft and forms a cap around the methyl group of leucine-18. Several waters in the cluster are hydrogen-bonded directly to the protein. Additional closed circular arrays, which include both protein atoms and other water oxygen atoms, form next to the central cluster. This water array stretches in the b lattice direction between groups of three ionic side chains.
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==About this Structure==
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Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin.,Teeter MM Proc Natl Acad Sci U S A. 1984 Oct;81(19):6014-6018. PMID:16593516<ref>PMID:16593516</ref>
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1CRN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CRN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin., Teeter MM, Proc Natl Acad Sci U S A. 1984 Oct;81(19):6014-6018. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16593516 16593516]
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</div>
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<div class="pdbe-citations 1crn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Crambe hispanica subsp. abyssinica]]
[[Category: Crambe hispanica subsp. abyssinica]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hendrickson, W.A.]]
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[[Category: Hendrickson WA]]
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[[Category: Teeter, M.M.]]
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[[Category: Teeter MM]]
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[[Category: plant seed protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:42:32 2007''
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WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC RESOLUTION. PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF CRAMBIN

PDB ID 1crn

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