1f9c

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[[Image:1f9c.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF MLE D178N VARIANT==
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|PDB= 1f9c |SIZE=350|CAPTION= <scene name='initialview01'>1f9c</scene>, resolution 2.50&Aring;
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<StructureSection load='1f9c' size='340' side='right'caption='[[1f9c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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<table><tr><td colspan='2'>[[1f9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9C FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Muconate_cycloisomerase Muconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.1 5.5.1.1] </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]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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|DOMAIN=
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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=1f9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9c OCA], [https://pdbe.org/1f9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9c RCSB], [https://www.ebi.ac.uk/pdbsum/1f9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9c ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1muc|1MUC]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9c OCA], [http://www.ebi.ac.uk/pdbsum/1f9c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f9c RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q51958_PSEPU Q51958_PSEPU]
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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/f9/1f9c_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=1f9c ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF MLE D178N VARIANT'''
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==See Also==
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*[[Muconate cycloisomerase|Muconate cycloisomerase]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: The traditional picture of charged amino acids in globular proteins is that they are almost exclusively on the outside exposed to the solvent. Buried charges, when they do occur, are assumed to play an essential role in catalysis and ligand binding, or in stabilizing structure as, for instance, helix caps. RESULTS: By analyzing the amount and distribution of buried charged surface and charges in proteins over a broad range of protein sizes, we show that buried charge is much more common than is generally believed. We also show that the amount of buried charge rises with protein size in a manner which differs from other types of surfaces, especially aromatic and polar uncharged surfaces. In large proteins such as hemocyanin, 35% of all charges are greater than 75% buried. Furthermore, at all sizes few charged groups are fully exposed. As an experimental test, we show that replacement of the buried D178 of muconate lactonizing enzyme by N stabilizes the enzyme by 4.2 degrees C without any change in crystallographic structure. In addition, free energy calculations of stability support the experimental results. CONCLUSIONS: Nature may use charge burial to reduce protein stability; not all buried charges are fully stabilized by a prearranged protein environment. Consistent with this view, thermophilic proteins often have less buried charge. Modifying the amount of buried charge at carefully chosen sites may thus provide a general route for changing the thermophilicity or psychrophilicity of proteins.
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[[Category: Large Structures]]
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==About this Structure==
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1F9C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9C OCA].
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==Reference==
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Buried charged surface in proteins., Kajander T, Kahn PC, Passila SH, Cohen DC, Lehtio L, Adolfsen W, Warwicker J, Schell U, Goldman A, Structure. 2000 Nov 15;8(11):1203-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080642 11080642]
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[[Category: Muconate cycloisomerase]]
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Goldman A]]
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[[Category: Goldman, A.]]
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[[Category: Kahn PC]]
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[[Category: Kahn, P C.]]
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[[Category: Kajander T]]
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[[Category: Kajander, T.]]
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[[Category: Lehtio L]]
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[[Category: Lehtio, L.]]
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[[Category: thermostable mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:18:25 2008''
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Current revision

CRYSTAL STRUCTURE OF MLE D178N VARIANT

PDB ID 1f9c

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