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1sqj
From Proteopedia
(New page: 200px<br /><applet load="1sqj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sqj, resolution 2.20Å" /> '''Crystal Structure An...) |
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| - | [[Image:1sqj.gif|left|200px]]<br /><applet load="1sqj" size=" | + | [[Image:1sqj.gif|left|200px]]<br /><applet load="1sqj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sqj, resolution 2.20Å" /> | caption="1sqj, resolution 2.20Å" /> | ||
'''Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)'''<br /> | '''Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC | + | Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1SQJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geotrichum_sp._m128 Geotrichum sp. m128]. Active as [http://en.wikipedia.org/wiki/Oligoxyloglucan_reducing-end-specific_cellobiohydrolase Oligoxyloglucan reducing-end-specific cellobiohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.150 3.2.1.150] Full crystallographic information is available from [http:// | + | 1SQJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geotrichum_sp._m128 Geotrichum sp. m128]. Active as [http://en.wikipedia.org/wiki/Oligoxyloglucan_reducing-end-specific_cellobiohydrolase Oligoxyloglucan reducing-end-specific cellobiohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.150 3.2.1.150] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:10 2008'' |
Revision as of 13:04, 21 February 2008
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Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)
Overview
Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.
About this Structure
1SQJ is a Single protein structure of sequence from Geotrichum sp. m128. Active as Oligoxyloglucan reducing-end-specific cellobiohydrolase, with EC number 3.2.1.150 Full crystallographic information is available from OCA.
Reference
Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase., Yaoi K, Kondo H, Noro N, Suzuki M, Tsuda S, Mitsuishi Y, Structure. 2004 Jul;12(7):1209-17. PMID:15242597
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