1ka2: Difference between revisions

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[[Image:1ka2.~~jpg~~|left|200px]]

[[Image:1ka2.png|left|200px]]

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~~'''~~Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg~~'''~~

===Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg===

~~==Overview==~~

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The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this ~~groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly~~, the ~~structure is similar~~ to the ~~recently reported rat neurolysin~~. ~~Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues~~. ~~The roles for these conserved residues in~~ the ~~catalytic mechanism are inferred based on modeling and their location~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11839307}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11839307 is the PubMed ID number.

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==About this Structure==

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[[Category: M32 family]]

[[Category: Metallopeptidase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:29:30 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:01:04 2008''

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-[[Image:1ka2.jpg|left|200px]]
+{{Seed}}
+[[Image:1ka2.png|left|200px]]
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 {{STRUCTURE_1ka2|  PDB=1ka2  |  SCENE=  }}
-'''Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg'''
+===Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg===
-==Overview==
+<!--
-The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.
+The line below this paragraph, {{ABSTRACT_PUBMED_11839307}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11839307 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11839307}}
 ==About this Structure==
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 [[Category: M32 family]]
 [[Category: Metallopeptidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:29:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:01:04 2008''