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| | {{STRUCTURE_1elm| PDB=1elm | SCENE= }} | | {{STRUCTURE_1elm| PDB=1elm | SCENE= }} |
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| - | '''CADMIUM-SUBSTITUTED BOVINE PACREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 5.5 AND 2 MM CHLORIDE IN MONOCLINIC CRYSTAL FORM.'''
| + | ===CADMIUM-SUBSTITUTED BOVINE PACREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 5.5 AND 2 MM CHLORIDE IN MONOCLINIC CRYSTAL FORM.=== |
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| - | ==Overview==
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| - | Three high-resolution crystal structures of Cd(II)-substituted carboxypeptidase A (CPA) have been determined by X-ray diffraction from crystals prepared in three different buffer systems to assess the effect of pH and ionic strength on the Cd(II) coordination geometry. All crystallize in the space group P2(1) with identical cell dimensions. Cd-CPA(7.5): Cd(II)-substituted CPA prepared at pH 7.5 with [Cl(-)]=2 mM determined to 1.70 A resolution ( R=17.4% and R(free)=19.8%); Cd-CPA(5.5): Cd(II)-substituted CPA prepared at pH 5.5 with [Cl(-)]=2 mM to 2.00 A resolution ( R=16.1% and R(free)=18.6%); Cd-CPA(7.5)-Cl: Cd(II)-substituted CPA prepared at pH 7.5 with [Cl(-)]=250 mM to 1.76 A resolution ( R=16.7% and R(free)=17.8%). No noticeable structural changes were observed between the three structures. Two water molecules coordinate to Cd(II), in contrast to the single water molecule coordinating to Zn(II) in the Zn-CPA structure. No binding sites for anions could be identified, even in the structure with a high concentration of chloride ions. It is suggested that the anion inhibition is due to weak outer-sphere association of Cl(-) ions at several binding sites, shielding the strong positive charge distribution at the surface of the protein near the active site. Based on structural data and a sequence alignment of 18 non-redundant carboxypeptidases, a more elaborate version of the earlier reaction model is proposed that also addresses the transport of water to and from the active site. Conserved residues whose function was not addressed previously delineate the proposed pathways used in the transport of water during catalysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11941507}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11941507 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11941507}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Larsen, S.]] | | [[Category: Larsen, S.]] |
| | [[Category: Alfa/beta fold]] | | [[Category: Alfa/beta fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:15:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:56:39 2008'' |
Revision as of 21:56, 30 June 2008
Template:STRUCTURE 1elm
CADMIUM-SUBSTITUTED BOVINE PACREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 5.5 AND 2 MM CHLORIDE IN MONOCLINIC CRYSTAL FORM.
Template:ABSTRACT PUBMED 11941507
About this Structure
1ELM is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Three high-resolution crystal structures of cadmium-substituted carboxypeptidase A provide insight into the enzymatic function., Jensen F, Bukrinsky T, Bjerrum J, Larsen S, J Biol Inorg Chem. 2002 Apr;7(4-5):490-9. Epub 2002 Feb 15. PMID:11941507
Page seeded by OCA on Tue Jul 1 00:56:39 2008
