1jjf
From Proteopedia
(New page: 200px<br /><applet load="1jjf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjf, resolution 1.75Å" /> '''STRUCTURAL BASIS FOR...) |
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| - | [[Image:1jjf.gif|left|200px]]<br /><applet load="1jjf" size=" | + | [[Image:1jjf.gif|left|200px]]<br /><applet load="1jjf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jjf, resolution 1.75Å" /> | caption="1jjf, resolution 1.75Å" /> | ||
'''STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERULOYL ESTERASE DOMAIN OF THE CELLULOSOMAL XYLANASE Z OF CLOSTRIDIUM THERMOCELLUM'''<br /> | '''STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERULOYL ESTERASE DOMAIN OF THE CELLULOSOMAL XYLANASE Z OF CLOSTRIDIUM THERMOCELLUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Feruloyl esterases function in the cleavage of ferulic acid's bonds to | + | Feruloyl esterases function in the cleavage of ferulic acid's bonds to arabinoxylan and pectin where the ferulic acid moieties cross-link the layers of polysaccharide chains within hemicellulose. This work presents the crystal structure of FAE_XynZ, the domain of Clostridium thermocellum's cellulosomal xylanase Z that displays feruloyl esterase activity. The structure was obtained via multiple isomorphous replacement with anomalous scattering (MIRAS) using three heavy atom derivatives and refined against X-ray diffraction data of up to 1.75 A resolution. The R-value of the final model was 0.187 (R(free) = 0.21). FAE_XynZ displays an eight-stranded alpha/beta-fold with the characteristic "catalytic triad" at the heart of the active site. To define the substrate specificity determinants of the enzyme, the crystal structures of FAE_XynZ and the inactive FAE_XynZ(S172A) mutant were determined in complexes with the feruloyl-arabinoxylans FAXX and FAX(3), respectively. In the complex crystals, the ferulic acid moieties are clearly recognizable and allowed identification of the hydrophobic binding pocket. The carbohydrate part of both substrates is not visible in either structure. The location of the putative carbohydrate binding-pocket was inferred based on the location and orientation of the adjacent ferulic acid molecule. Five of the six residues lining the pocket were found to be conserved in FAE A from Orpinomyces sp., which further supports the proposed role of these amino acids. |
==About this Structure== | ==About this Structure== | ||
| - | 1JJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with PT as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1JJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with <scene name='pdbligand=PT:'>PT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blum, D | + | [[Category: Blum, D L.]] |
| - | [[Category: Kataeva, I | + | [[Category: Kataeva, I A.]] |
| - | [[Category: Ljungdahl, L | + | [[Category: Ljungdahl, L G.]] |
| - | [[Category: Rose, J | + | [[Category: Rose, J P.]] |
| - | [[Category: SECSG, Southeast | + | [[Category: SECSG, Southeast Collaboratory for Structural Genomics.]] |
| - | [[Category: Schubot, F | + | [[Category: Schubot, F D.]] |
| - | [[Category: Shah, A | + | [[Category: Shah, A K.]] |
| - | [[Category: Wang, B | + | [[Category: Wang, B C.]] |
[[Category: PT]] | [[Category: PT]] | ||
[[Category: fae_xynz]] | [[Category: fae_xynz]] | ||
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[[Category: xynz]] | [[Category: xynz]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:23 2008'' |
Revision as of 11:23, 21 February 2008
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STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERULOYL ESTERASE DOMAIN OF THE CELLULOSOMAL XYLANASE Z OF CLOSTRIDIUM THERMOCELLUM
Overview
Feruloyl esterases function in the cleavage of ferulic acid's bonds to arabinoxylan and pectin where the ferulic acid moieties cross-link the layers of polysaccharide chains within hemicellulose. This work presents the crystal structure of FAE_XynZ, the domain of Clostridium thermocellum's cellulosomal xylanase Z that displays feruloyl esterase activity. The structure was obtained via multiple isomorphous replacement with anomalous scattering (MIRAS) using three heavy atom derivatives and refined against X-ray diffraction data of up to 1.75 A resolution. The R-value of the final model was 0.187 (R(free) = 0.21). FAE_XynZ displays an eight-stranded alpha/beta-fold with the characteristic "catalytic triad" at the heart of the active site. To define the substrate specificity determinants of the enzyme, the crystal structures of FAE_XynZ and the inactive FAE_XynZ(S172A) mutant were determined in complexes with the feruloyl-arabinoxylans FAXX and FAX(3), respectively. In the complex crystals, the ferulic acid moieties are clearly recognizable and allowed identification of the hydrophobic binding pocket. The carbohydrate part of both substrates is not visible in either structure. The location of the putative carbohydrate binding-pocket was inferred based on the location and orientation of the adjacent ferulic acid molecule. Five of the six residues lining the pocket were found to be conserved in FAE A from Orpinomyces sp., which further supports the proposed role of these amino acids.
About this Structure
1JJF is a Single protein structure of sequence from Clostridium thermocellum with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum., Schubot FD, Kataeva IA, Blum DL, Shah AK, Ljungdahl LG, Rose JP, Wang BC, Biochemistry. 2001 Oct 23;40(42):12524-32. PMID:11601976
Page seeded by OCA on Thu Feb 21 13:23:23 2008
Categories: Clostridium thermocellum | Endo-1,4-beta-xylanase | Single protein | Blum, D L. | Kataeva, I A. | Ljungdahl, L G. | Rose, J P. | SECSG, Southeast Collaboratory for Structural Genomics. | Schubot, F D. | Shah, A K. | Wang, B C. | PT | Fae xynz | Ferulic acid esterase | Feruloyl esterase | Protein structure initiative | Psi | Secsg | Southeast collaboratory for structural genomics | Structural genomics | Xynz
