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| [[Image:1qd6.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1qd6.png|left|200px]] |
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| {{STRUCTURE_1qd6| PDB=1qd6 | SCENE= }} | | {{STRUCTURE_1qd6| PDB=1qd6 | SCENE= }} |
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| '''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI'''
| | ===OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI=== |
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| ==Overview==
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| Dimerization is a biological regulatory mechanism employed by both soluble and membrane proteins. However, there are few structural data on the factors that govern dimerization of membrane proteins. Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme which participates in secretion of colicins in Escherichia coli. In Campilobacter and Helicobacter pylori strains, OMPLA is implied in virulence. Its activity is regulated by reversible dimerization. Here we report X-ray structures of monomeric and dimeric OMPLA from E. coli. Dimer interactions occur almost exclusively in the apolar membrane-embedded parts, with two hydrogen bonds within the hydrophobic membrane area being key interactions. Dimerization results in functional oxyanion holes and substrate-binding pockets, which are absent in monomeric OMPLA. These results provide a detailed view of activation by dimerization of a membrane protein.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10537112}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10537112 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10537112}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Verheij, H M.]] | | [[Category: Verheij, H M.]] |
| [[Category: Anti-parallel beta barrel dimer]] | | [[Category: Anti-parallel beta barrel dimer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:09:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:57:42 2008'' |