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1bxb

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Revision as of 08:07, 29 November 2017

XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS

Structural highlights

1bxb is a 4 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	XYLA (THET8)
Activity:	Xylose isomerase, with EC number 5.3.1.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 highly thermostable xylose isomerases from Thermus thermophilus (TthXI) and Thermus caldophilus (TcaXI), both with the optimum reaction temperature of 90 degrees C, have been determined by X-ray crystallography. The model of TcaXI has been refined to an R-factor of 17.8 % for data extending to 2.3 A and that of TthXI to 17.1 % for data extending to 2.2 A. The tetrameric arrangement of subunits characterized by the 222-symmetry and the tertiary fold of each subunit in both TcaXI and TthXI are basically the same as in other xylose isomerases. Each monomer is composed of two domains. Domain I (residues 1 to 321) folds into the (beta/alpha)8-barrel. Domain II (residues 322 to 387), lacking beta-strands, makes extensive contacts with domain I of an adjacent subunit. Each monomer of TcaXI contains ten beta-strands, 15 alpha-helices, and six 310-helices, while that of TthXI contains ten beta-strands, 16 alpha-helices, and five 310-helices. Although the electron density does not indicate the presence of bound metal ions in the present models of both TcaXI and TthXI, the active site residues show the conserved structural features. In order to understand the structural basis for thermostability of these enzymes, their structures have been compared with less thermostable XIs from Arthrobacter B3728 and Actinoplanes missouriensis (AXI and AmiXI), with the optimum reaction temperatures of 80 degrees C and 75 degrees C, respectively. Analyses of various factors that may affect protein thermostability indicate that the possible structural determinants of the enhanced thermostability of TcaXI/TthXI over AXI/AmiXI are (i) an increase in ion pairs and ion-pair networks, (ii) a decrease in the large inter-subunit cavities, (iii) a removal of potential deamidation/isoaspartate formation sites, and (iv) a shortened loop.

Crystal structures of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability.,Chang C, Park BC, Lee DS, Suh SW J Mol Biol. 1999 May 14;288(4):623-34. PMID:10329168^[1]

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

References

↑ Chang C, Park BC, Lee DS, Suh SW. Crystal structures of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability. J Mol Biol. 1999 May 14;288(4):623-34. PMID:10329168 doi:10.1006/jmbi.1999.2696

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS==
 <StructureSection load='1bxb' size='340' side='right' caption='[[1bxb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XYLA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=1bxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxb OCA], [http://pdbe.org/1bxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bxb RCSB], [http://www.ebi.ac.uk/pdbsum/1bxb PDBsum]</span></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=1bxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxb OCA], [http://pdbe.org/1bxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bxb RCSB], [http://www.ebi.ac.uk/pdbsum/1bxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxb ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 26: / Line 27: @@
 </div>
 <div class="pdbe-citations 1bxb" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[D-xylose isomerase|D-xylose isomerase]]
 == References ==
 <references/>

1bxb

From Proteopedia

Revision as of 08:07, 29 November 2017

XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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