1g9k
From Proteopedia
(New page: 200px<br /><applet load="1g9k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g9k, resolution 1.96Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1g9k.jpg|left|200px]]<br /><applet load="1g9k" size=" | + | [[Image:1g9k.jpg|left|200px]]<br /><applet load="1g9k" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g9k, resolution 1.96Å" /> | caption="1g9k, resolution 1.96Å" /> | ||
'''CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18'''<br /> | '''CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enzymes from psychrophilic organisms differ from their mesophilic | + | Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a conformation as in the substrate-bound form of the mesophilic proteases. Further, a region in the catalytic domain of PAP undergoes a conformational change with a loop movement as large as 13 A, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions. |
==About this Structure== | ==About this Structure== | ||
| - | 1G9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas Pseudomonas] with CA, SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] Full crystallographic information is available from [http:// | + | 1G9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas Pseudomonas] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G9K OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta jelly roll]] | [[Category: beta jelly roll]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:39 2008'' |
Revision as of 10:47, 21 February 2008
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CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18
Overview
Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a conformation as in the substrate-bound form of the mesophilic proteases. Further, a region in the catalytic domain of PAP undergoes a conformational change with a loop movement as large as 13 A, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions.
About this Structure
1G9K is a Single protein structure of sequence from Pseudomonas with , and as ligands. Active as Serralysin, with EC number 3.4.24.40 Full crystallographic information is available from OCA.
Reference
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases., Aghajari N, Van Petegem F, Villeret V, Chessa JP, Gerday C, Haser R, Van Beeumen J, Proteins. 2003 Mar 1;50(4):636-47. PMID:12577270
Page seeded by OCA on Thu Feb 21 12:47:39 2008
Categories: Pseudomonas | Serralysin | Single protein | Aghajari, N. | Haser, R. | CA | SO4 | ZN | Beta jelly roll
