1myl

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[[Image:1myl.gif|left|200px]]
 
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{{Structure
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==SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY==
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|PDB= 1myl |SIZE=350|CAPTION= <scene name='initialview01'>1myl</scene>, resolution 2.4&Aring;
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<StructureSection load='1myl' size='340' side='right'caption='[[1myl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1myl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYL FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.4&#8491;</td></tr>
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|GENE= MUTATED ARC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 Enterobacteria phage P22])
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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=1myl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myl OCA], [https://pdbe.org/1myl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myl RCSB], [https://www.ebi.ac.uk/pdbsum/1myl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myl ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1myl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myl OCA], [http://www.ebi.ac.uk/pdbsum/1myl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1myl RCSB]</span>
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[https://www.uniprot.org/uniprot/RARC_BPP22 RARC_BPP22] This protein acts as a transcriptional repressor of its own gene arc and of gene ant.
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}}
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'''SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY'''
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==See Also==
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*[[Myosin 3D Structures|Myosin 3D Structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity.
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[[Category: Large Structures]]
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[[Category: Salmonella virus P22]]
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==About this Structure==
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[[Category: Sauer RT]]
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1MYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYL OCA].
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[[Category: Schildbach JF]]
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[[Category: Waldburger CD]]
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==Reference==
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Are buried salt bridges important for protein stability and conformational specificity?, Waldburger CD, Schildbach JF, Sauer RT, Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7749916 7749916]
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[[Category: Enterobacteria phage p22]]
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[[Category: Single protein]]
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[[Category: Sauer, R T.]]
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[[Category: Schildbach, J F.]]
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[[Category: Waldburger, C D.]]
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[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:57 2008''
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Current revision

SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY

PDB ID 1myl

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