1xas: Difference between revisions

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New page: left|200px<br /><applet load="1xas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xas, resolution 2.6Å" /> '''CRYSTAL STRUCTURE, AT...
 
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[[Image:1xas.gif|left|200px]]<br /><applet load="1xas" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xas, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES'''<br />


==Overview==
==CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES==
The crystal structure of the 32-kDa catalytic domain of the Streptomyces, lividans xylanase A was solved by molecular isomorphous replacement, methods and subsequently refined at 2.6-A resolution to a conventional, crystallographic R factor of 0.21. This is the first successful structure, determination of a member of the F family of endo-beta-1,4-D-glycanases., Unlike the recently determined xylanases of the G family (Wakarchuk, W., W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994), Protein Sci. 3, 467-475), where the catalytic domains have a unique, beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is, folded into a complete (alpha/beta)8 barrel, the first such fold observed, among beta-1,4-D-glycanases. The active site is located at the carbonyl, end of the beta barrel. The crystal structure supports the earlier, assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R., (1994) Biochem. J., in press).
<StructureSection load='1xas' size='340' side='right'caption='[[1xas]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1xas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XAS FirstGlance]. <br>
1XAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XAS OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=1xas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xas OCA], [https://pdbe.org/1xas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xas RCSB], [https://www.ebi.ac.uk/pdbsum/1xas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xas ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases., Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS, J Biol Chem. 1994 Aug 19;269(33):20811-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8063693 8063693]
== Function ==
[[Category: Endo-1,4-beta-xylanase]]
[https://www.uniprot.org/uniprot/XYNA_STRLI XYNA_STRLI] Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
[[Category: Single protein]]
== 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/xa/1xas_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=1xas ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
[[Category: Derewenda, U.]]
[[Category: Derewenda U]]
[[Category: Derewenda, Z.S.]]
[[Category: Derewenda ZS]]
[[Category: xylanase a]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:57:00 2007''

Latest revision as of 11:49, 14 February 2024

CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSESCRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES

Structural highlights

1xas is a 1 chain structure with sequence from Streptomyces lividans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

XYNA_STRLI Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.

Evolutionary Conservation

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

1xas, resolution 2.60Å

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