1mh3: Difference between revisions

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[[Image:1mh3.jpg|left|200px]]


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==maltose binding-a1 homeodomain protein chimera, crystal form I==
The line below this paragraph, containing "STRUCTURE_1mh3", creates the "Structure Box" on the page.
<StructureSection load='1mh3' size='340' side='right'caption='[[1mh3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1mh3]] is a 1 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=1MH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MH3 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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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=1mh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mh3 OCA], [https://pdbe.org/1mh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mh3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mh3 ProSAT]</span></td></tr>
{{STRUCTURE_1mh3|  PDB=1mh3  |  SCENE= }}
</table>
 
== Function ==
'''maltose binding-a1 homeodomain protein chimera, crystal form I'''
[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/HMRA1_YEAST HMRA1_YEAST] Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of A1 at HMR.
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
The Yeast MATa1 and MATalpha2 are homeodomain proteins that bind DNA cooperatively to repress transcription of cell type specific genes. The DNA affinity and specificity of MATa1 in the absence of MATalpha2, however, is very low. MATa1 is converted to a higher affinity DNA-binding protein by its interaction with the C-terminal tail of MATalpha2. To understand why MATa1 binds DNA weakly by itself, and how the MATalpha2 tail affects the affinity of MATa1 for DNA, we determined the crystal structure of a maltose-binding protein (MBP)-a1 chimera whose DNA binding behavior is similar to MATa1. The overall MATa1 conformation in the MBP-a1 structure, which was determined in the absence of alpha2 and DNA, is similar to that in the a1/alpha2/DNA structure. The sole difference is in the C-terminal portion of the DNA recognition helix of MATa1, which is flexible in the present structure. However, these residues are not in a location likely to be affected by binding of the MATalpha2 tail. The results argue against conformational changes in a1 induced by the tail of MATalpha2, suggesting instead that the MATalpha2 tail energetically couples the DNA binding of MATalpha2 and MATa1.
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mh/1mh3_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1MH3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_and_saccharomyces_cerevisiae Escherichia coli and saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MH3 OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=1mh3 ConSurf].
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera., Ke A, Wolberger C, Protein Sci. 2003 Feb;12(2):306-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12538894 12538894]
<div style="clear:both"></div>
[[Category: Escherichia coli and saccharomyces cerevisiae]]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Ke, A.]]
[[Category: Escherichia coli]]
[[Category: Wolberger, C.]]
[[Category: Large Structures]]
[[Category: Binding cooperativity]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Homeodomain]]
[[Category: Ke A]]
[[Category: Maltose binding protein]]
[[Category: Wolberger C]]
[[Category: Mata1]]
[[Category: Mbp]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:00:45 2008''

Latest revision as of 10:43, 14 February 2024

maltose binding-a1 homeodomain protein chimera, crystal form Imaltose binding-a1 homeodomain protein chimera, crystal form I

Structural highlights

1mh3 is a 1 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.
Method:X-ray diffraction, Resolution 2.1Å
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.HMRA1_YEAST Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of A1 at HMR.

Evolutionary Conservation

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

1mh3, resolution 2.10Å

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