Peptidoglycan binding domains have a general

peptidoglycan Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like layer (sacculus) that surrounds the bacterial cytoplasmic membrane. The sugar component consists of alternating ...

binding function and a common core structure consisting of a closed, three-helical bundle with a left-handed twist. It is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. Examples are: * Muramoyl-pentapeptide carboxypeptidase () * N-acetylmuramoyl-L-alanine amidase cwlA precursor (cell wall hydrolase, autolysin, ) * Autolytic lysozyme (1,4-beta-N-acetylmuramidase, autolysin, ) * Membrane-bound lytic murein transglycosylase B * Zinc-containing D-alanyl-D-alanine-cleaving carboxypeptidase, VanX. Many of the proteins having this domain are as yet uncharacterised. However, some are known to belong to MEROPS peptidase family M15 (clan MD), subfamily M15A metallopeptidases. A number of the proteins belonging to subfamily M15A are non-peptidase homologues as they either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity. Eukaryotic enzymes can contain structurally similar PGBD-like domains. Matrix metalloproteinases (MMP), which catalyse extracellular matrix degradation, have N-terminal domains that resemble PGBD. Examples are gelatinase A (MMP-2), which degrades type IV collagen, stromelysin-1 (MMP-3), which plays a role in arthritis and tumour invasion, and gelatinase B (MMP-9) secreted by neutrophils as part of the innate immune defence mechanism. Several MMPs are implicated in cancer progression, since degradation of the extracellular matrix is an essential step in the cascade of metastasis.

Examples

Humans genes encoding proteins containing this domain include: *

MMP1 Interstitial collagenase, also known as fibroblast collagenase and matrix metalloproteinase-1 (MMP-1), is an enzyme that in humans is encoded by the ''MMP1'' gene. The gene is part of a cluster of MMP genes which localize to 11q, chromosome 11q2 ...

MMP2 72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the ''MMP2'' gene. The ''MMP2'' gene is located on chromosome 16 at position 12.2. Function Proteins of the ...

MMP3 Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the ''MMP3'' gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-3 has an estimated molecular we ...

, MMP7,

MMP8 Neutrophil collagenase, also known as matrix metalloproteinase-8 (MMP-8) or PMNL collagenase (MNL-CL), is a collagen cleaving enzyme which is present in the connective tissue of most mammals. In humans, the MMP-8 protein is encoded by the ''MMP ...

MMP9 Matrix metalloproteinase-9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extrac ...

, *

MMP10 Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the ''MMP10'' gene. Function Proteins of the matrix metalloproteinase ( MMP) family are involved in the breakdown of extrac ...

MMP12 Matrix metalloproteinase-12 (MMP-12) also known as macrophage metalloelastase (MME) or macrophage elastase (ME) is an enzyme that in humans is encoded by the ''MMP12'' gene. Function Proteins of the matrix metalloproteinase (MMP) family are inv ...

, MMP13, MMP14, MMP15, MMP16, MMP17, MMP19, * MMP20, MMP21, MMP24, MMP25, MMP27, MMP28

References

{{InterPro content, IPR002477 Protein domains Single-pass transmembrane proteins