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New page: left|200px<br /><applet load="1bhw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhw, resolution 4.1Å" /> '''LOW TEMPERATURE MIDDL...
 
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[[Image:1bhw.jpg|left|200px]]<br /><applet load="1bhw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bhw, resolution 4.1&Aring;" />
'''LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF XYLOSE ISOMERASE FROM MASC DATA'''<br />


==Overview==
==LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF XYLOSE ISOMERASE FROM MASC DATA==
A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48], presented the theoretical foundations of MASC, a new contrast-variation, method using multiwavelength anomalous scattering, and reported the first, experimental results. New experiments have been conducted both at the ESRF, (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled, crystals of three proteins of known structures and very different, molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure, factors of the anomalously scattering part of the crystal including the, solvent zone and the ordered anomalous scattering sites (if any), have, been extracted from multiwavelength data. In the very low resolution range, (d &gt;/= 20 A), the agreement between experimental {GammaT(h)} and model, values calculated from the bulk solvent is all the more satisfactory since, the molecular weight of the protein is high. For spacings between 10 and, 20 A, the agreement between experimental {GammaT(h)} and model values is, also satisfactory if one takes into account ordered anomalous scatterer, sites. Such sites have been found in the three cases.
<StructureSection load='1bhw' size='340' side='right'caption='[[1bhw]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bhw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.1&#8491;</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=1bhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhw OCA], [https://pdbe.org/1bhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhw RCSB], [https://www.ebi.ac.uk/pdbsum/1bhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYLA_ACTM4 XYLA_ACTM4]
== 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/bh/1bhw_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=1bhw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d &gt;/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.


==About this Structure==
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.,Ramin M, Shepard W, Fourme R, Kahn R Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999, Jan 1. PMID:10089406<ref>PMID:10089406</ref>
1BHW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BHW OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values., Ramin M, Shepard W, Fourme R, Kahn R, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999, Jan 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10089406 10089406]
</div>
<div class="pdbe-citations 1bhw" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinoplanes missouriensis]]
[[Category: Actinoplanes missouriensis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Xylose isomerase]]
[[Category: Fourme R]]
[[Category: Fourme, R.]]
[[Category: Kahn R]]
[[Category: Kahn, R.]]
[[Category: Ramin M]]
[[Category: Ramin, M.]]
[[Category: Shepard W]]
[[Category: Shepard, W.]]
[[Category: isomerase]]
[[Category: masc]]
[[Category: multiwavelength anomalous solvent contrast]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:40:02 2007''

Latest revision as of 11:02, 2 August 2023

LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF XYLOSE ISOMERASE FROM MASC DATA

1bhw, resolution 4.10Å

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