1nmu

From Proteopedia

(Difference between revisions)

Revision as of 09:47, 21 December 2022

MBP-L30

Structural highlights

1nmu is a 4 chain structure with sequence from Escherichia coli and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chao JA, Prasad GS, White SA, Stout CD, Williamson JR. Inherent protein structural flexibility at the RNA-binding interface of L30e. J Mol Biol. 2003 Feb 28;326(4):999-1004. PMID:12589748

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nmu"

@@ Line 3: / Line 3: @@
 <StructureSection load='1nmu' size='340' side='right'caption='[[1nmu]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1nmu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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>
+<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>
-</td></tr><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></td></tr>
+</td></tr><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>
 <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>
 </table>
 == Function ==
-[[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.
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Chao, J A]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Prasad, G S]]
+[[Category: Chao JA]]
-[[Category: Stout, C D]]
+[[Category: Prasad GS]]
-[[Category: White, S A]]
+[[Category: Stout CD]]
-[[Category: Williamson, J R]]
+[[Category: White SA]]
-[[Category: Mbp-l30 fusion protein]]
+[[Category: Williamson JR]]
-[[Category: Ribosomal protein l30]]
-[[Category: Structural flexibility]]
-[[Category: Sugar binding protein-ribosome complex]]

1nmu

From Proteopedia

Revision as of 09:47, 21 December 2022

MBP-L30

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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