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| - | [[Image:1loc.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1loc| PDB=1loc | SCENE= }} | | {{STRUCTURE_1loc| PDB=1loc | SCENE= }} |
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| - | '''INTERACTION OF A LEGUME LECTIN WITH TWO COMPONENTS OF THE BACTERIAL CELL WALL'''
| + | ===INTERACTION OF A LEGUME LECTIN WITH TWO COMPONENTS OF THE BACTERIAL CELL WALL=== |
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| - | ==Overview==
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| - | We describe herein the refined high resolution x-ray structures of two components of the bacterial cell wall, muramic acid and muramyl dipeptide complexed to isolectin I from Lathyrus ochrus seeds. In both complexes, only the ring hydroxyl oxygen atoms of the bound sugar establish direct hydrogen bonds with isolectin I, as in the case of all the previously determined monosaccharide-lectin complexes. In addition, the lactyl methyl of both components strongly interacts via hydrophobic contacts with the side chains of residues Tyr100 and Trp128 of isolectin I, which could explain the higher affinity of isolectin I for muramic acid as compared with glucose. These 2 residues, however, are not involved in the stabilization of the oligosaccharide-isolectin I complexes. The dipeptide (D-Ala-D-iGln) of the second component is in stacking interaction with the N-acetyl group of glucose and with loop Gly97-Gly98 of isolectin I. In addition to these van der Waals' contacts, the dipeptide interacts with the lectin via well ordered water molecules also. Superposition of the structures of the muramyl dipeptide complex and of the muramic acid complex shows that the glucose ring in the dipeptide compound is tilted by about 15 degrees in comparison with that of muramic acid. The fact that the lactyl group has the same confrontation in both components reveals that the lectin is stereospecific and recognizes only diastereoisomer S of this group, which better fits the saccharide-binding site.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8144527}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8144527 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8144527}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Cambillau, C.]] | | [[Category: Cambillau, C.]] |
| | [[Category: Lectin]] | | [[Category: Lectin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:06:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:34:56 2008'' |
Revision as of 18:34, 2 July 2008
Template:STRUCTURE 1loc
INTERACTION OF A LEGUME LECTIN WITH TWO COMPONENTS OF THE BACTERIAL CELL WALL
Template:ABSTRACT PUBMED 8144527
About this Structure
1LOC is a Protein complex structure of sequences from Lathyrus ochrus. Full crystallographic information is available from OCA.
Reference
Interaction of a legume lectin with two components of the bacterial cell wall. A crystallographic study., Bourne Y, Ayouba A, Rouge P, Cambillau C, J Biol Chem. 1994 Apr 1;269(13):9429-35. PMID:8144527
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