1h71
From Proteopedia
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| - | [[Image:1h71.gif|left|200px]]<br /><applet load="1h71" size=" | + | [[Image:1h71.gif|left|200px]]<br /><applet load="1h71" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h71, resolution 2.1Å" /> | caption="1h71, resolution 2.1Å" /> | ||
'''PSYCHROPHILIC PROTEASE FROM PSEUDOALTEROMONAS 'TAC II 18''''<br /> | '''PSYCHROPHILIC PROTEASE FROM PSEUDOALTEROMONAS 'TAC II 18''''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40. 3.4.24.40.] Known structural/functional Site: <scene name='pdbsite=ZNB:Ca Binding Site For Residue P507'>ZNB</scene>. Full crystallographic information is available from [http:// | + | 1H71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40. 3.4.24.40.] Known structural/functional Site: <scene name='pdbsite=ZNB:Ca+Binding+Site+For+Residue+P507'>ZNB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H71 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: psychrophilic]] | [[Category: psychrophilic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:11 2008'' |
Revision as of 07:47, 3 February 2008
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PSYCHROPHILIC PROTEASE FROM PSEUDOALTEROMONAS '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
1H71 is a Single protein structure of sequence from Bacteria with and as ligands. Active as Hydrolase, with EC number 3.4.24.40. Known structural/functional Site: . 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
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