2hpo
From Proteopedia
(New page: 200px<br /><applet load="2hpo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hpo, resolution 1.65Å" /> '''Structure of Aminope...) |
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| - | [[Image:2hpo.gif|left|200px]]<br /><applet load="2hpo" size=" | + | [[Image:2hpo.gif|left|200px]]<br /><applet load="2hpo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hpo, resolution 1.65Å" /> | caption="2hpo, resolution 1.65Å" /> | ||
'''Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site'''<br /> | '''Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aminopeptidase N from Escherichia coli is a major metalloprotease that | + | Aminopeptidase N from Escherichia coli is a major metalloprotease that participates in the controlled hydrolysis of peptides in the proteolytic pathway. Determination of the 870-aa structure reveals that it has four domains similar to the tricorn-interacting factor F3. The thermolysin-like active site is enclosed within a large cavity with a volume of 2,200 A(3), which is inaccessible to substrates except for a small opening of approximately 8-10 A. The substrate-based inhibitor bestatin binds to the protein with minimal changes, suggesting that this is the active form of the enzyme. The previously described structure of F3 had three distinct conformations that were described as "closed," "intermediate," and "open." The structure of aminopeptidase N from E. coli, however, is substantially more closed than any of these. Taken together, the results suggest that these proteases, which are involved in intracellular peptide degradation, prevent inadvertent hydrolysis of inappropriate substrates by enclosing the active site within a large cavity. There is also some evidence that the open form of the enzyme, which admits substrates, remains inactive until it adopts the closed form. |
==About this Structure== | ==About this Structure== | ||
| - | 2HPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] Full crystallographic information is available from [http:// | + | 2HPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Addlagatta, A.]] | [[Category: Addlagatta, A.]] | ||
[[Category: Gay, L.]] | [[Category: Gay, L.]] | ||
| - | [[Category: Matthews, B | + | [[Category: Matthews, B W.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: multidomain]] | [[Category: multidomain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:24 2008'' |
Revision as of 15:44, 21 February 2008
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Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site
Overview
Aminopeptidase N from Escherichia coli is a major metalloprotease that participates in the controlled hydrolysis of peptides in the proteolytic pathway. Determination of the 870-aa structure reveals that it has four domains similar to the tricorn-interacting factor F3. The thermolysin-like active site is enclosed within a large cavity with a volume of 2,200 A(3), which is inaccessible to substrates except for a small opening of approximately 8-10 A. The substrate-based inhibitor bestatin binds to the protein with minimal changes, suggesting that this is the active form of the enzyme. The previously described structure of F3 had three distinct conformations that were described as "closed," "intermediate," and "open." The structure of aminopeptidase N from E. coli, however, is substantially more closed than any of these. Taken together, the results suggest that these proteases, which are involved in intracellular peptide degradation, prevent inadvertent hydrolysis of inappropriate substrates by enclosing the active site within a large cavity. There is also some evidence that the open form of the enzyme, which admits substrates, remains inactive until it adopts the closed form.
About this Structure
2HPO is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Membrane alanyl aminopeptidase, with EC number 3.4.11.2 Full crystallographic information is available from OCA.
Reference
Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site., Addlagatta A, Gay L, Matthews BW, Proc Natl Acad Sci U S A. 2006 Sep 5;103(36):13339-44. Epub 2006 Aug 28. PMID:16938892
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