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1f0w

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[[Image:1f0w.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5==
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The line below this paragraph, containing "STRUCTURE_1f0w", creates the "Structure Box" on the page.
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<StructureSection load='1f0w' size='340' side='right'caption='[[1f0w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1f0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F0W FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#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=1f0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0w OCA], [https://pdbe.org/1f0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0w RCSB], [https://www.ebi.ac.uk/pdbsum/1f0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0w ProSAT]</span></td></tr>
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{{STRUCTURE_1f0w| PDB=1f0w | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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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/f0/1f0w_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=1f0w ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5'''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Overview==
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<references/>
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The structure analyses of orthorhombic lysozyme grown at pH 6.5 and its low-humidity variant are reported. The structures of the same form grown at pH 9.5 and 4.5 and that of the low-humidity variant of the pH 9.5 form are available. A comparison between them shows that the changes in molecular geometry and hydration caused by changes in the amount of solvent surrounding protein molecules are more pronounced than those caused by variation in pH. In particular, the conformation and the mutual orientation of the catalytic residues Glu35 and Asp52 remain unaffected by change in pH. A comparative study involving 20 crystallographically independent lysozyme molecules, including five in the orthorhombic form, leads to the delineation of the relatively rigid, moderately flexible and highly flexible regions of the molecule. Half the binding cleft (subsites D, E and F) belong to the rigid region but the other half (subsites A, B and C) belong to a flexible region. There is no marked correlation between relative rigidity and conservation of side-chain conformation except at the binding site. The study permits the identification of seven invariant water molecules associated with the protein. Most of them are involved in important tertiary interactions, while one occurs in the active-site cleft. The study demonstrates a weak correlation between non-accessibility and rigidity. On average, the level of hydration of polar atoms increases rapidly with accessible atomic surface area, but levels off at about 15 A(2) at a little over one ordered water molecule per polar protein atom. Only 15 N and O atoms are hydrated in all 20 molecules. 13 of these are hydrated by the seven invariant water molecules. Of the seven, only one water molecule is totally buried within the protein.
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__TOC__
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</StructureSection>
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==About this Structure==
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1F0W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0W OCA].
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==Reference==
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Hydration, mobility and accessibility of lysozyme: structures of a pH 6.5 orthorhombic form and its low-humidity variant and a comparative study involving 20 crystallographically independent molecules., Biswal BK, Sukumar N, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1110-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10957630 10957630]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Biswal BK]]
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[[Category: Biswal, B K.]]
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[[Category: Sukumar N]]
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[[Category: Sukumar, N.]]
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[[Category: Vijayan M]]
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[[Category: Vijayan, M.]]
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[[Category: Enzyme-orthorhombic form]]
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[[Category: Glycosidase]]
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[[Category: Hen egg-white lysozyme]]
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[[Category: Mucopeptide n-acetylmuramyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:45:37 2008''
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Current revision

CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5

PDB ID 1f0w

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