1f5j: Difference between revisions

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[[Image:1f5j.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF XYNB, A HIGHLY THERMOSTABLE BETA-1,4-XYLANASE FROM DICTYOGLOMUS THERMOPHILUM RT46B.1, AT 1.8 A RESOLUTION==
|PDB= 1f5j |SIZE=350|CAPTION= <scene name='initialview01'>1f5j</scene>, resolution 1.80&Aring;
<StructureSection load='1f5j' size='340' side='right'caption='[[1f5j]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1f5j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyoglomus_thermophilum Dictyoglomus thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F5J FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5j OCA], [https://pdbe.org/1f5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f5j RCSB], [https://www.ebi.ac.uk/pdbsum/1f5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f5j ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5j OCA], [http://www.ebi.ac.uk/pdbsum/1f5j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f5j RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/P77853_DICTH P77853_DICTH]
 
== Evolutionary Conservation ==
'''CRYSTAL STRUCTURE OF XYNB, A HIGHLY THERMOSTABLE BETA-1,4-XYLANASE FROM DICTYOGLOMUS THERMOPHILUM RT46B.1, AT 1.8 A RESOLUTION'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/1f5j_consurf.spt"</scriptWhenChecked>
Microorganisms employ a large array of enzymes to break down the cellulose and hemicelluloses of plant biomass. These enzymes, especially those with high thermal stability, have many uses in biotechnology. We have solved the crystal structure of a beta-1, 4-xylanase, XynB, from the extremely thermophilic bacterium Dictyoglomus thermophilum, isolate Rt46B.1. The protein crystallized from 1.6 M ammonium sulfate, 0.2 M HEPES pH 7.2 and 10% glycerol, with unit-cell parameters a = b = 91.3, c = 44.9 A and space group P4(3). The structure was solved at high resolution (1.8 A) by X-ray crystallography, using the method of isomorphous replacement with a single mercury derivative, and refined to a final R factor of 18.3% (R(free) = 22.1%). XynB has the single-domain fold typical of family 11 xylanases, comprising a jelly roll of two highly twisted beta-sheets that create a deep substrate-binding cleft. The two catalytic residues, Glu90 and Glu180, occupy this cleft. Compared with other family 11 xylanases, XynB has a greater proportion of polar surface and has a slightly extended C-terminus that, combined with the extension of beta-strand A5, gives additional hydrogen bonding and hydrophobic packing. These factors may account for the enhanced thermal stability of the enzyme.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1F5J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyoglomus_thermophilum Dictyoglomus thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5J OCA].  
</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=1f5j ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Structure of XynB, a highly thermostable beta-1,4-xylanase from Dictyoglomus thermophilum Rt46B.1, at 1.8 A resolution., McCarthy AA, Morris DD, Bergquist PL, Baker EN, Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1367-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11053833 11053833]
</StructureSection>
[[Category: Dictyoglomus thermophilum]]
[[Category: Dictyoglomus thermophilum]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Baker EN]]
[[Category: Baker, E N.]]
[[Category: McCarthy AA]]
[[Category: McCarthy, A A.]]
[[Category: beta-barrel]]
[[Category: xylanase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:20 2008''

Latest revision as of 10:10, 7 February 2024

CRYSTAL STRUCTURE OF XYNB, A HIGHLY THERMOSTABLE BETA-1,4-XYLANASE FROM DICTYOGLOMUS THERMOPHILUM RT46B.1, AT 1.8 A RESOLUTIONCRYSTAL STRUCTURE OF XYNB, A HIGHLY THERMOSTABLE BETA-1,4-XYLANASE FROM DICTYOGLOMUS THERMOPHILUM RT46B.1, AT 1.8 A RESOLUTION

Structural highlights

1f5j is a 2 chain structure with sequence from Dictyoglomus thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

P77853_DICTH

Evolutionary Conservation

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

1f5j, resolution 1.80Å

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