1m4w

From Proteopedia

(Difference between revisions)

Current revision

Thermophilic b-1,4-xylanase from Nonomuraea flexuosa

Structural highlights

1m4w is a 1 chain structure with sequence from Thermopolyspora flexuosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8GMV7_9ACTN

Evolutionary Conservation

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

Publication Abstract from PubMed

The crystal structures of thermophilic xylanases from Chaetomium thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A resolution, respectively. Both enzymes have the overall fold typical to family 11 xylanases with two highly twisted beta-sheets forming a large cleft. The comparison of 12 crystal structures of family 11 xylanases from both mesophilic and thermophilic organisms showed that the structures of different xylanases are very similar. The sequence identity differences correlated well with the structural differences. Several minor modifications appeared to be responsible for the increased thermal stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased number of charged residues, especially Arg, resulting in enhanced polar interactions, and (c) improved stabilization of secondary structures involved the higher number of residues in the beta-strands and stabilization of the alpha-helix region. Some members of family 11 xylanases have a unique strategy to improve their stability, such as a higher number of ion pairs or aromatic residues on protein surface, a more compact structure, a tighter packing, and insertions at some regions resulting in enhanced interactions.

Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability.,Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J Eur J Biochem. 2003 Apr;270(7):1399-412. PMID:12653995^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J. Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability. Eur J Biochem. 2003 Apr;270(7):1399-412. PMID:12653995

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m4w"

@@ Line 1: / Line 1: @@
 ==Thermophilic b-1,4-xylanase from Nonomuraea flexuosa==
-<StructureSection load='1m4w' size='340' side='right' caption='[[1m4w]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='1m4w' size='340' side='right'caption='[[1m4w]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m4w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"acetomadura_flexuosa"_krasil'nikov_and_agre_1964 "acetomadura flexuosa" krasil'nikov and agre 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M4W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1m4w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermopolyspora_flexuosa Thermopolyspora flexuosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4W FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4w OCA], [http://pdbe.org/1m4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m4w RCSB], [http://www.ebi.ac.uk/pdbsum/1m4w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4w ProSAT]</span></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=1m4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4w OCA], [https://pdbe.org/1m4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4w RCSB], [https://www.ebi.ac.uk/pdbsum/1m4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4w ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8GMV7_9ACTN Q8GMV7_9ACTN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/1m4w_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Acetomadura flexuosa krasil'nikov and agre 1964]]
+[[Category: Large Structures]]
-[[Category: Endo-1,4-beta-xylanase]]
+[[Category: Thermopolyspora flexuosa]]
-[[Category: Hakulinen, N]]
+[[Category: Hakulinen N]]
-[[Category: Janis, J]]
+[[Category: Janis J]]
-[[Category: Leisola, M]]
+[[Category: Leisola M]]
-[[Category: Rouvinen, J]]
+[[Category: Rouvinen J]]
-[[Category: Turunen, O]]
+[[Category: Turunen O]]
-[[Category: Family 11]]
-[[Category: Glycosyl hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Thermostability]]
-[[Category: Xylanase]]

1m4w

From Proteopedia

Current revision

Thermophilic b-1,4-xylanase from Nonomuraea flexuosa

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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