RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica
Background: The Lipase Engineering Database (LED) integrates information on sequence, structure and function of lipases, esterases and related proteins with the a/b hydrolase fold. A new superfamily for Candida antarctica lipase A (CALA) was introduced including the recently published crystal struct...
Main Authors: | , , , |
---|---|
Other Authors: | |
Format: | Text |
Language: | English |
Subjects: | |
Online Access: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.354.3859 |
id |
ftciteseerx:oai:CiteSeerX.psu:10.1.1.354.3859 |
---|---|
record_format |
openpolar |
spelling |
ftciteseerx:oai:CiteSeerX.psu:10.1.1.354.3859 2023-05-15T13:32:25+02:00 RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica Lipase A Michael Widmann P Benjamin Juhl Jürgen Pleiss The Pennsylvania State University CiteSeerX Archives application/zip http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.354.3859 en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.354.3859 Metadata may be used without restrictions as long as the oai identifier remains attached to it. ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/88/d5/BMC_Genomics_2010_Feb_19_11_123.tar.gz text ftciteseerx 2016-01-08T00:29:55Z Background: The Lipase Engineering Database (LED) integrates information on sequence, structure and function of lipases, esterases and related proteins with the a/b hydrolase fold. A new superfamily for Candida antarctica lipase A (CALA) was introduced including the recently published crystal structure of CALA. Since CALA has a highly divergent sequence in comparison to other a/b hydrolases, the Lipase Engineering Database was used to classify CALA in the frame of the already established classification system. This involved the comparison of CALA to similar structures as well as sequence-based comparisons against the content of the LED. Results: The new release 3.0 (December 2009) of the Lipase Engineering Database contains 24783 sequence entries for 18585 proteins as well as 656 experimentally determined protein structures, including the structure of CALA. In comparison to the previous release [1] with 4322 protein and 167 structure entries this update represents a significant increase in data volume. By comparing CALA to representative structures from all superfamilies, a structure from the deacetylase superfamily was found to be most similar to the structure of CALA. While the a/b hydrolase fold is conserved in both proteins, the major difference is found in the cap region. Sequence alignments between both proteins show a sequence similarity of only 15%. A multisequence alignment of both protein families was used to create hidden Markov models for the cap region of CALA and showed that the cap region of CALA is unique among all other proteins of the a/b hydrolase fold. By specifically comparing the substrate binding pocket of CALA to other binding pockets of a/b hydrolases, the binding pocket of Candida rugosa lipase was identified as being highly similar. This similarity also applied to the lid of Candida rugosa lipase in comparison to the potential lid of CALA. Conclusion: The LED serves as a valuable tool for the systematic analysis of single proteins or protein families. The updated release 3.0 was used ... Text Antarc* Antarctica Unknown Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
institution |
Open Polar |
collection |
Unknown |
op_collection_id |
ftciteseerx |
language |
English |
description |
Background: The Lipase Engineering Database (LED) integrates information on sequence, structure and function of lipases, esterases and related proteins with the a/b hydrolase fold. A new superfamily for Candida antarctica lipase A (CALA) was introduced including the recently published crystal structure of CALA. Since CALA has a highly divergent sequence in comparison to other a/b hydrolases, the Lipase Engineering Database was used to classify CALA in the frame of the already established classification system. This involved the comparison of CALA to similar structures as well as sequence-based comparisons against the content of the LED. Results: The new release 3.0 (December 2009) of the Lipase Engineering Database contains 24783 sequence entries for 18585 proteins as well as 656 experimentally determined protein structures, including the structure of CALA. In comparison to the previous release [1] with 4322 protein and 167 structure entries this update represents a significant increase in data volume. By comparing CALA to representative structures from all superfamilies, a structure from the deacetylase superfamily was found to be most similar to the structure of CALA. While the a/b hydrolase fold is conserved in both proteins, the major difference is found in the cap region. Sequence alignments between both proteins show a sequence similarity of only 15%. A multisequence alignment of both protein families was used to create hidden Markov models for the cap region of CALA and showed that the cap region of CALA is unique among all other proteins of the a/b hydrolase fold. By specifically comparing the substrate binding pocket of CALA to other binding pockets of a/b hydrolases, the binding pocket of Candida rugosa lipase was identified as being highly similar. This similarity also applied to the lid of Candida rugosa lipase in comparison to the potential lid of CALA. Conclusion: The LED serves as a valuable tool for the systematic analysis of single proteins or protein families. The updated release 3.0 was used ... |
author2 |
The Pennsylvania State University CiteSeerX Archives |
format |
Text |
author |
Lipase A Michael Widmann P Benjamin Juhl Jürgen Pleiss |
spellingShingle |
Lipase A Michael Widmann P Benjamin Juhl Jürgen Pleiss RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica |
author_facet |
Lipase A Michael Widmann P Benjamin Juhl Jürgen Pleiss |
author_sort |
Lipase A |
title |
RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica |
title_short |
RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica |
title_full |
RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica |
title_fullStr |
RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica |
title_full_unstemmed |
RESEARCH ARTICLE Open Access Structural classification by the Lipase Engineering Database: a case study of Candida antarctica |
title_sort |
research article open access structural classification by the lipase engineering database: a case study of candida antarctica |
url |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.354.3859 |
long_lat |
ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
geographic |
Rugosa |
geographic_facet |
Rugosa |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/88/d5/BMC_Genomics_2010_Feb_19_11_123.tar.gz |
op_relation |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.354.3859 |
op_rights |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
_version_ |
1766026946907471872 |