1qtr
From Proteopedia
(New page: 200px<br /><applet load="1qtr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qtr, resolution 2.32Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1qtr.jpg|left|200px]]<br /><applet load="1qtr" size=" | + | [[Image:1qtr.jpg|left|200px]]<br /><applet load="1qtr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qtr, resolution 2.32Å" /> | caption="1qtr, resolution 2.32Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the | + | Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 A resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline. |
==About this Structure== | ==About this Structure== | ||
| - | 1QTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Active as [http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] Full crystallographic information is available from [http:// | + | 1QTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Active as [http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTR OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of prolyl aminopeptidase from Serratia marcescens., Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K, J Biochem | + | Crystal structure of prolyl aminopeptidase from Serratia marcescens., Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K, J Biochem. 1999 Sep;126(3):559-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10467172 10467172] |
[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
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[[Category: serratia]] | [[Category: serratia]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:36 2008'' |
Revision as of 12:43, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS
Overview
Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 A resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline.
About this Structure
1QTR is a Single protein structure of sequence from Serratia marcescens. Active as Prolyl aminopeptidase, with EC number 3.4.11.5 Full crystallographic information is available from OCA.
Reference
Crystal structure of prolyl aminopeptidase from Serratia marcescens., Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K, J Biochem. 1999 Sep;126(3):559-65. PMID:10467172
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