1nmu

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{{Seed}}
 
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[[Image:1nmu.png|left|200px]]
 
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==MBP-L30==
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The line below this paragraph, containing "STRUCTURE_1nmu", creates the "Structure Box" on the page.
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<StructureSection load='1nmu' size='340' side='right'caption='[[1nmu]], [[Resolution|resolution]] 2.31&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'>[[1nmu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NMU 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]] 2.31&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr>
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{{STRUCTURE_1nmu| PDB=1nmu | SCENE= }}
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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=1nmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nmu OCA], [https://pdbe.org/1nmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nmu RCSB], [https://www.ebi.ac.uk/pdbsum/1nmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nmu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
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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/nm/1nmu_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=1nmu 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 Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein with two copies in the asymmetric unit has been determined. The flexible RNA-binding region in the L30 copies has two distinct conformations, one resembles the RNA bound form solved by NMR and the other is unique. Structure prediction algorithms also had difficulty accurately predicting this region, which is consistent with conformational flexibility seen in the NMR and X-ray crystallography studies. Inherent conformational flexibility may be a hallmark of regions involved in intermolecular interactions.
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===MBP-L30===
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Inherent protein structural flexibility at the RNA-binding interface of L30e.,Chao JA, Prasad GS, White SA, Stout CD, Williamson JR J Mol Biol. 2003 Feb 28;326(4):999-1004. PMID:12589748<ref>PMID:12589748</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1nmu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12589748}}, adds the Publication Abstract to the page
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*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12589748 is the PubMed ID number.
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*[[Ribosomal protein L30|Ribosomal protein L30]]
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== References ==
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{{ABSTRACT_PUBMED_12589748}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1NMU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMU OCA].
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==Reference==
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Inherent protein structural flexibility at the RNA-binding interface of L30e., Chao JA, Prasad GS, White SA, Stout CD, Williamson JR, J Mol Biol. 2003 Feb 28;326(4):999-1004. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12589748 12589748]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Chao, J A.]]
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[[Category: Chao JA]]
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[[Category: Prasad, G S.]]
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[[Category: Prasad GS]]
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[[Category: Stout, C D.]]
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[[Category: Stout CD]]
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[[Category: White, S A.]]
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[[Category: White SA]]
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[[Category: Williamson, J R.]]
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[[Category: Williamson JR]]
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[[Category: Mbp-l30 fusion protein]]
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[[Category: Ribosomal protein l30]]
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[[Category: Structural flexibility]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:29:55 2008''
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Current revision

MBP-L30

PDB ID 1nmu

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