2h25: Difference between revisions

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[[Image:2h25.jpg|left|200px]]
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{{STRUCTURE_2h25|  PDB=2h25  |  SCENE=  }}
'''Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin'''


==Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin==
<StructureSection load='2h25' size='340' side='right'caption='[[2h25]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2h25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H25 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h25 OCA], [https://pdbe.org/2h25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h25 RCSB], [https://www.ebi.ac.uk/pdbsum/2h25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h25 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h25_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2h25 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins &lt;30 kDa, although global fold determination is possible for substantially larger proteins. Here we present a strategy for assigning backbone and side-chain resonances of large proteins without deuteration, with which one can obtain high-resolution structures from (1)H-(1)H distance restraints. The strategy uses information from through-bond correlation experiments to filter intraresidue and sequential correlations from through-space correlation experiments, and then matches the filtered correlations to obtain sequential assignment. We demonstrate this strategy on three proteins ranging from 24 to 65 kDa for resonance assignment and on maltose binding protein (42 kDa) and hemoglobin (65 kDa) for high-resolution structure determination. The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling.


==Overview==
A new strategy for structure determination of large proteins in solution without deuteration.,Xu Y, Zheng Y, Fan JS, Yang D Nat Methods. 2006 Nov;3(11):931-7. PMID:17060917<ref>PMID:17060917</ref>
So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins &lt;30 kDa, although global fold determination is possible for substantially larger proteins. Here we present a strategy for assigning backbone and side-chain resonances of large proteins without deuteration, with which one can obtain high-resolution structures from (1)H-(1)H distance restraints. The strategy uses information from through-bond correlation experiments to filter intraresidue and sequential correlations from through-space correlation experiments, and then matches the filtered correlations to obtain sequential assignment. We demonstrate this strategy on three proteins ranging from 24 to 65 kDa for resonance assignment and on maltose binding protein (42 kDa) and hemoglobin (65 kDa) for high-resolution structure determination. The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2H25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H25 OCA].
</div>
<div class="pdbe-citations 2h25" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
A new strategy for structure determination of large proteins in solution without deuteration., Xu Y, Zheng Y, Fan JS, Yang D, Nat Methods. 2006 Nov;3(11):931-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17060917 17060917]
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Lin, Z.]]
[[Category: Lin Z]]
[[Category: Xu, Y.]]
[[Category: Xu Y]]
[[Category: Yang, D.]]
[[Category: Yang D]]
[[Category: Zheng, Y.]]
[[Category: Zheng Y]]
[[Category: Alpha/beta protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:46:58 2008''

Latest revision as of 19:00, 29 May 2024

Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin

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